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  1. Article ; Online: Architecture of the flexible tail tube of bacteriophage SPP1

    Maximilian Zinke / Katrin A. A. Sachowsky / Carl Öster / Sophie Zinn-Justin / Raimond Ravelli / Gunnar F. Schröder / Michael Habeck / Adam Lange

    Nature Communications, Vol 11, Iss 1, Pp 1-

    2020  Volume 9

    Abstract: Bacteriophages of the Siphoviridae family have a long, flexible, non-contractile tail that has been difficult to characterize structurally. Here, the authors present the atomic structure of the tail tube of one of these phages, showing a hollow flexible ... ...

    Abstract Bacteriophages of the Siphoviridae family have a long, flexible, non-contractile tail that has been difficult to characterize structurally. Here, the authors present the atomic structure of the tail tube of one of these phages, showing a hollow flexible tube formed by hexameric rings stacked by flexible linkers.
    Keywords Science ; Q
    Language English
    Publishing date 2020-11-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: Architecture of the flexible tail tube of bacteriophage SPP1

    Maximilian Zinke / Katrin A. A. Sachowsky / Carl Öster / Sophie Zinn-Justin / Raimond Ravelli / Gunnar F. Schröder / Michael Habeck / Adam Lange

    Nature Communications, Vol 11, Iss 1, Pp 1-

    2020  Volume 9

    Abstract: Bacteriophages of the Siphoviridae family have a long, flexible, non-contractile tail that has been difficult to characterize structurally. Here, the authors present the atomic structure of the tail tube of one of these phages, showing a hollow flexible ... ...

    Abstract Bacteriophages of the Siphoviridae family have a long, flexible, non-contractile tail that has been difficult to characterize structurally. Here, the authors present the atomic structure of the tail tube of one of these phages, showing a hollow flexible tube formed by hexameric rings stacked by flexible linkers.
    Keywords Science ; Q
    Language English
    Publishing date 2020-11-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: Structural plasticity of the selectivity filter in a nonselective ion channel

    Raktim N. Roy / Kitty Hendriks / Wojciech Kopec / Saeid Abdolvand / Kevin L. Weiss / Bert L. de Groot / Adam Lange / Han Sun / Leighton Coates

    IUCrJ, Vol 8, Iss 3, Pp 421-

    2021  Volume 430

    Abstract: The sodium potassium ion channel (NaK) is a nonselective ion channel that conducts both sodium and potassium across the cellular membrane. A new crystallographic structure of NaK reveals conformational differences in the residues that make up the ... ...

    Abstract The sodium potassium ion channel (NaK) is a nonselective ion channel that conducts both sodium and potassium across the cellular membrane. A new crystallographic structure of NaK reveals conformational differences in the residues that make up the selectivity filter between the four subunits that form the ion channel and the inner helix of the ion channel. The crystallographic structure also identifies a side-entry, ion-conduction pathway for Na+ permeation that is unique to NaK. NMR studies and molecular dynamics simulations confirmed the dynamical nature of the top part of the selectivity filter and the inner helix in NaK as also observed in the crystal structure. Taken together, these results indicate that the structural plasticity of the selectivity filter combined with the dynamics of the inner helix of NaK are vital for the efficient conduction of different ions through the non-selective ion channel of NaK.
    Keywords ion channels ; membrane proteins ; x-ray crystallography ; solid-state nmr ; molecular dynamics ; Science ; Q
    Subject code 572
    Language English
    Publishing date 2021-05-01T00:00:00Z
    Publisher International Union of Crystallography
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: A single NaK channel conformation is not enough for non-selective ion conduction

    Chaowei Shi / Yao He / Kitty Hendriks / Bert L. de Groot / Xiaoying Cai / Changlin Tian / Adam Lange / Han Sun

    Nature Communications, Vol 9, Iss 1, Pp 1-

    2018  Volume 8

    Abstract: NaK is a non-selective cation channel that conducts sodium (Na+) and potassium (K+) equally well. Here authors use ssNMR and MD simulations to show that the selectivity filter of NaK adopts two conformations in the absence of ions, one of which is ... ...

    Abstract NaK is a non-selective cation channel that conducts sodium (Na+) and potassium (K+) equally well. Here authors use ssNMR and MD simulations to show that the selectivity filter of NaK adopts two conformations in the absence of ions, one of which is preferred by Na+ and the other by K+.
    Keywords Science ; Q
    Language English
    Publishing date 2018-02-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: A single NaK channel conformation is not enough for non-selective ion conduction

    Chaowei Shi / Yao He / Kitty Hendriks / Bert L. de Groot / Xiaoying Cai / Changlin Tian / Adam Lange / Han Sun

    Nature Communications, Vol 9, Iss 1, Pp 1-

    2018  Volume 8

    Abstract: NaK is a non-selective cation channel that conducts sodium (Na+) and potassium (K+) equally well. Here authors use ssNMR and MD simulations to show that the selectivity filter of NaK adopts two conformations in the absence of ions, one of which is ... ...

    Abstract NaK is a non-selective cation channel that conducts sodium (Na+) and potassium (K+) equally well. Here authors use ssNMR and MD simulations to show that the selectivity filter of NaK adopts two conformations in the absence of ions, one of which is preferred by Na+ and the other by K+.
    Keywords Science ; Q
    Language English
    Publishing date 2018-02-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  6. Article: Spontaneous Aggregation of the Insulin-Derived Steric Zipper Peptide VEALYL Results in Different Aggregation Forms with Common Features

    Matthes, Dirk / Venita Daebel / Karsten Meyenberg / Dietmar Riedel / Gudrun Heim / Ulf Diederichsen / Adam Lange / Bert L. de Groot

    Journal of Molecular Biology. 2014 Jan. 23, v. 426

    2014  

    Abstract: Recently, several short peptides have been shown to self-assemble into amyloid fibrils with generic cross-β spines, so-called steric zippers, suggesting common underlying structural features and aggregation mechanisms. Understanding these mechanisms is ... ...

    Abstract Recently, several short peptides have been shown to self-assemble into amyloid fibrils with generic cross-β spines, so-called steric zippers, suggesting common underlying structural features and aggregation mechanisms. Understanding these mechanisms is a prerequisite for designing fibril-binding compounds and inhibitors of fibril formation. The hexapeptide VEALYL, corresponding to the residues B12-17 of full-length insulin, has been identified as one of these short segments. Here, we analyzed the structures of multiple, morphologically different (fibrillar, microcrystal-like, oligomeric) [13C,15N]VEALYL samples by solid-state nuclear magnetic resonance complemented with results from molecular dynamics simulations. By performing NHHC/CHHC experiments, we could determine that the β-strands within a given sheet of the amyloid-like fibrils formed by the insulin hexapeptide VEALYL are stacked in an antiparallel manner, whereas the sheet-to-sheet packing arrangement was found to be parallel. Experimentally observed secondary chemical shifts for all aggregate forms, as well as ∅ and ψ backbone torsion angles calculated with TALOS, are indicative of β-strand conformation, consistent with the published crystal structure (PDB ID: 2OMQ). Thus, we could demonstrate that the structural features of all the observed VEALYL aggregates are in agreement with the previously observed homosteric zipper spine packing in the crystalline state, suggesting that several distinct aggregate morphologies share the same molecular architecture.
    Keywords amyloid ; crystal structure ; insulin ; molecular dynamics ; nuclear magnetic resonance spectroscopy ; peptides
    Language English
    Dates of publication 2014-0123
    Size p. 362-376.
    Publishing place Elsevier Ltd
    Document type Article
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2013.10.020
    Database NAL-Catalogue (AGRICOLA)

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    Z 4' 63/108: Show issues

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  7. Article: Emerin self‐assembly mechanism: role of the LEM domain

    Samson, Camille / Adam Lange / Ana‐Andreea Arteni / Béatrice Alpha‐Bazin / Catherine Coirault / Florian Celli / François‐Xavier Theillet / Isaline Herrada / Jean Armengaud / Kitty Hendriks / Maximilian Zinke / Nada Essawy / Sophie Zinn‐Justin

    FEBS journal. 2017 Jan., v. 284, no. 2

    2017  

    Abstract: At the nuclear envelope, the inner nuclear membrane protein emerin contributes to the interface between the nucleoskeleton and the chromatin. Emerin is an essential actor of the nuclear response to a mechanical signal. Genetic defects in emerin cause ... ...

    Abstract At the nuclear envelope, the inner nuclear membrane protein emerin contributes to the interface between the nucleoskeleton and the chromatin. Emerin is an essential actor of the nuclear response to a mechanical signal. Genetic defects in emerin cause Emery–Dreifuss muscular dystrophy. It was proposed that emerin oligomerization regulates nucleoskeleton binding, and impaired oligomerization contributes to the loss of function of emerin disease‐causing mutants. We here report the first structural characterization of emerin oligomers. We identified an N‐terminal emerin region from amino acid 1 to amino acid 132 that is necessary and sufficient for formation of long curvilinear filaments. In emerin monomer, this region contains a globular LEM domain and a fragment that is intrinsically disordered. Solid‐state nuclear magnetic resonance analysis identifies the LEM β‐fragment as part of the oligomeric structural core. However, the LEM domain alone does not self‐assemble into filaments. Additional residues forming a β‐structure are observed within the filaments that could correspond to the unstructured region in emerin monomer. We show that the delK37 mutation causing muscular dystrophy triggers LEM domain unfolding and increases emerin self‐assembly rate. Similarly, inserting a disulfide bridge that stabilizes the LEM folded state impairs emerin N‐terminal region self‐assembly, whereas reducing this disulfide bridge triggers self‐assembly. We conclude that the LEM domain, responsible for binding to the chromatin protein BAF, undergoes a conformational change during self‐assembly of emerin N‐terminal region. The consequences of these structural rearrangement and self‐assembly events on emerin binding properties are discussed.
    Keywords amino acids ; binding properties ; chromatin ; disulfide bonds ; membrane proteins ; muscular dystrophy ; mutants ; mutation ; nuclear magnetic resonance spectroscopy ; nuclear membrane ; oligomerization
    Language English
    Dates of publication 2017-01
    Size p. 338-352.
    Publishing place John Wiley & Sons, Ltd
    Document type Article
    Note JOURNAL ARTICLE
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/febs.13983
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 2006/704: Show issues

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  8. Article ; Online: NMR-based detection of hydrogen/deuterium exchange in liposome-embedded membrane proteins.

    Xuejun Yao / Ulrich H N Dürr / Zrinka Gattin / Yvonne Laukat / Rhagavendran L Narayanan / Ann-Kathrin Brückner / Chris Meisinger / Adam Lange / Stefan Becker / Markus Zweckstetter

    PLoS ONE, Vol 9, Iss 11, p e

    2014  Volume 112374

    Abstract: Membrane proteins play key roles in biology. Determination of their structure in a membrane environment, however, is highly challenging. To address this challenge, we developed an approach that couples hydrogen/deuterium exchange of membrane proteins to ... ...

    Abstract Membrane proteins play key roles in biology. Determination of their structure in a membrane environment, however, is highly challenging. To address this challenge, we developed an approach that couples hydrogen/deuterium exchange of membrane proteins to rapid unfolding and detection by solution-state NMR spectroscopy. We show that the method allows analysis of the solvent protection of single residues in liposome-embedded proteins such as the 349-residue Tom40, the major protein translocation pore in the outer mitochondrial membrane, which has resisted structural analysis for many years.
    Keywords Medicine ; R ; Science ; Q
    Language English
    Publishing date 2014-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  9. Article ; Online: The common structural architecture of Shigella flexneri and Salmonella typhimurium type three secretion needles.

    Jean-Philippe Demers / Nikolaos G Sgourakis / Rashmi Gupta / Antoine Loquet / Karin Giller / Dietmar Riedel / Britta Laube / Michael Kolbe / David Baker / Stefan Becker / Adam Lange

    PLoS Pathogens, Vol 9, Iss 3, p e

    2013  Volume 1003245

    Abstract: The Type Three Secretion System (T3SS), or injectisome, is a macromolecular infection machinery present in many pathogenic Gram-negative bacteria. It consists of a basal body, anchored in both bacterial membranes, and a hollow needle through which ... ...

    Abstract The Type Three Secretion System (T3SS), or injectisome, is a macromolecular infection machinery present in many pathogenic Gram-negative bacteria. It consists of a basal body, anchored in both bacterial membranes, and a hollow needle through which effector proteins are delivered into the target host cell. Two different architectures of the T3SS needle have been previously proposed. First, an atomic model of the Salmonella typhimurium needle was generated from solid-state NMR data. The needle subunit protein, PrgI, comprises a rigid-extended N-terminal segment and a helix-loop-helix motif with the N-terminus located on the outside face of the needle. Second, a model of the Shigella flexneri needle was generated from a high-resolution 7.7-Å cryo-electron microscopy density map. The subunit protein, MxiH, contains an N-terminal α-helix, a loop, another α-helix, a 14-residue-long β-hairpin (Q51-Q64) and a C-terminal α-helix, with the N-terminus facing inward to the lumen of the needle. In the current study, we carried out solid-state NMR measurements of wild-type Shigella flexneri needles polymerized in vitro and identified the following secondary structure elements for MxiH: a rigid-extended N-terminal segment (S2-T11), an α-helix (L12-A38), a loop (E39-P44) and a C-terminal α-helix (Q45-R83). Using immunogold labeling in vitro and in vivo on functional needles, we located the N-terminus of MxiH subunits on the exterior of the assembly, consistent with evolutionary sequence conservation patterns and mutagenesis data. We generated a homology model of Shigella flexneri needles compatible with both experimental data: the MxiH solid-state NMR chemical shifts and the state-of-the-art cryoEM density map. These results corroborate the solid-state NMR structure previously solved for Salmonella typhimurium PrgI needles and establish that Shigella flexneri and Salmonella typhimurium subunit proteins adopt a conserved structure and orientation in their assembled state. Our study reveals a common structural architecture of T3SS needles, essential to understand T3SS-mediated infection and develop treatments.
    Keywords Immunologic diseases. Allergy ; RC581-607 ; Biology (General) ; QH301-705.5
    Subject code 572
    Language English
    Publishing date 2013-03-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  10. Article ; Online: High-resolution 3D structure determination of kaliotoxin by solid-state NMR spectroscopy.

    Jegannath Korukottu / Robert Schneider / Vinesh Vijayan / Adam Lange / Olaf Pongs / Stefan Becker / Marc Baldus / Markus Zweckstetter

    PLoS ONE, Vol 3, Iss 6, p e

    2008  Volume 2359

    Abstract: High-resolution solid-state NMR spectroscopy can provide structural information of proteins that cannot be studied by X-ray crystallography or solution NMR spectroscopy. Here we demonstrate that it is possible to determine a protein structure by solid- ... ...

    Abstract High-resolution solid-state NMR spectroscopy can provide structural information of proteins that cannot be studied by X-ray crystallography or solution NMR spectroscopy. Here we demonstrate that it is possible to determine a protein structure by solid-state NMR to a resolution comparable to that by solution NMR. Using an iterative assignment and structure calculation protocol, a large number of distance restraints was extracted from (1)H/(1)H mixing experiments recorded on a single uniformly labeled sample under magic angle spinning conditions. The calculated structure has a coordinate precision of 0.6 A and 1.3 A for the backbone and side chain heavy atoms, respectively, and deviates from the structure observed in solution. The approach is expected to be applicable to larger systems enabling the determination of high-resolution structures of amyloid or membrane proteins.
    Keywords Medicine ; R ; Science ; Q
    Language English
    Publishing date 2008-06-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
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