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  1. Article ; Online: Structure of the MRAS-SHOC2-PP1C phosphatase complex.

    Hauseman, Zachary J / Fodor, Michelle / Dhembi, Anxhela / Viscomi, Jessica / Egli, David / Bleu, Melusine / Katz, Stephanie / Park, Eunyoung / Jang, Dong Man / Porter, Kathryn A / Meili, Fabian / Guo, Hongqiu / Kerr, Grainne / Mollé, Sandra / Velez-Vega, Camilo / Beyer, Kim S / Galli, Giorgio G / Maira, Saveur-Michel / Stams, Travis /
    Clark, Kirk / Eck, Michael J / Tordella, Luca / Thoma, Claudio R / King, Daniel A

    Nature

    2022  Volume 609, Issue 7926, Page(s) 416–423

    Abstract: RAS-MAPK signalling is fundamental for cell proliferation and is altered in most human ... ...

    Abstract RAS-MAPK signalling is fundamental for cell proliferation and is altered in most human cancers
    MeSH term(s) 14-3-3 Proteins ; Crystallography, X-Ray ; Guanosine Triphosphate/metabolism ; Humans ; Intracellular Signaling Peptides and Proteins/chemistry ; Intracellular Signaling Peptides and Proteins/metabolism ; MAP Kinase Signaling System ; Multiprotein Complexes/chemistry ; Mutation ; Protein Isoforms/chemistry ; Protein Isoforms/metabolism ; Protein Phosphatase 1/chemistry ; Protein Phosphatase 1/genetics ; Protein Phosphatase 1/metabolism ; Protein Subunits/chemistry ; Protein Subunits/metabolism ; raf Kinases ; ras Proteins/chemistry ; ras Proteins/metabolism
    Chemical Substances 14-3-3 Proteins ; Intracellular Signaling Peptides and Proteins ; MRAS protein, human ; Multiprotein Complexes ; Protein Isoforms ; Protein Subunits ; SHOC2 protein, human ; Guanosine Triphosphate (86-01-1) ; raf Kinases (EC 2.7.11.1) ; Protein Phosphatase 1 (EC 3.1.3.16) ; ras Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2022-07-13
    Publishing country England
    Document type Journal Article
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/s41586-022-05086-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Snapshots of C-S Cleavage in Egt2 Reveals Substrate Specificity and Reaction Mechanism.

    Irani, Seema / Naowarojna, Nathchar / Tang, Yang / Kathuria, Karan R / Wang, Shu / Dhembi, Anxhela / Lee, Norman / Yan, Wupeng / Lyu, Huijue / Costello, Catherine E / Liu, Pinghua / Zhang, Yan Jessie

    Cell chemical biology

    2018  Volume 25, Issue 5, Page(s) 519–529.e4

    Abstract: Sulfur incorporation in the biosynthesis of ergothioneine, a histidine thiol derivative, differs from other well-characterized transsulfurations. A combination of a mononuclear non-heme iron enzyme-catalyzed oxidative C-S bond formation and a subsequent ... ...

    Abstract Sulfur incorporation in the biosynthesis of ergothioneine, a histidine thiol derivative, differs from other well-characterized transsulfurations. A combination of a mononuclear non-heme iron enzyme-catalyzed oxidative C-S bond formation and a subsequent pyridoxal 5'-phosphate (PLP)-mediated C-S lyase reaction leads to the net transfer of a sulfur atom from a cysteine to a histidine. In this study, we structurally and mechanistically characterized a PLP-dependent C-S lyase Egt2, which mediates the sulfoxide C-S bond cleavage in ergothioneine biosynthesis. A cation-π interaction between substrate and enzyme accounts for Egt2's preference of sulfoxide over thioether as a substrate. Using mutagenesis and structural biology, we captured three distinct states of the Egt2 C-S lyase reaction cycle, including a labile sulfenic intermediate captured in Egt2 crystals. Chemical trapping and high-resolution mass spectrometry were used to confirm the involvement of the sulfenic acid intermediate in Egt2 catalysis.
    MeSH term(s) Biosynthetic Pathways ; Catalytic Domain ; Crystallography, X-Ray ; Ergothioneine/metabolism ; Fungal Proteins/chemistry ; Fungal Proteins/metabolism ; Lyases/chemistry ; Lyases/metabolism ; Neurospora crassa/chemistry ; Neurospora crassa/metabolism ; Protein Conformation ; Pyridoxal Phosphate/metabolism ; Substrate Specificity ; Sulfenic Acids/metabolism
    Chemical Substances Fungal Proteins ; Sulfenic Acids ; Pyridoxal Phosphate (5V5IOJ8338) ; Ergothioneine (BDZ3DQM98W) ; Lyases (EC 4.-)
    Language English
    Publishing date 2018-03-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 2451-9448
    ISSN (online) 2451-9448
    DOI 10.1016/j.chembiol.2018.02.002
    Database MEDical Literature Analysis and Retrieval System OnLINE

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