Artikel ; Online: Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis.
Nature structural & molecular biology
2020 Band 27, Heft 5, Seite(n) 406–416
Abstract: The ClpAP complex is a conserved bacterial protease that unfolds and degrades proteins targeted for destruction. The ClpA double-ring hexamer powers substrate unfolding and translocation into the ClpP proteolytic chamber. Here, we determined high- ... ...
Abstract | The ClpAP complex is a conserved bacterial protease that unfolds and degrades proteins targeted for destruction. The ClpA double-ring hexamer powers substrate unfolding and translocation into the ClpP proteolytic chamber. Here, we determined high-resolution structures of wild-type Escherichia coli ClpAP undergoing active substrate unfolding and proteolysis. A spiral of pore loop-substrate contacts spans both ClpA AAA+ domains. Protomers at the spiral seam undergo nucleotide-specific rearrangements, supporting substrate translocation. IGL loops extend flexibly to bind the planar, heptameric ClpP surface with the empty, symmetry-mismatched IGL pocket maintained at the seam. Three different structures identify a binding-pocket switch by the IGL loop of the lowest positioned protomer, involving release and re-engagement with the clockwise pocket. This switch is coupled to a ClpA rotation and a network of conformational changes across the seam, suggesting that ClpA can rotate around the ClpP apical surface during processive steps of translocation and proteolysis. |
---|---|
Mesh-Begriff(e) | Adenosine Triphosphate/analogs & derivatives ; Adenosine Triphosphate/metabolism ; Cryoelectron Microscopy ; DNA Helicases/metabolism ; Endopeptidase Clp/chemistry ; Endopeptidase Clp/genetics ; Endopeptidase Clp/metabolism ; Escherichia coli/chemistry ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Models, Molecular ; Multiprotein Complexes ; Protein Conformation ; Protein Unfolding ; Trans-Activators/metabolism |
Chemische Substanzen | Escherichia coli Proteins ; Multiprotein Complexes ; Trans-Activators ; replication initiator protein ; adenosine 5'-O-(3-thiotriphosphate) (35094-46-3) ; Adenosine Triphosphate (8L70Q75FXE) ; ClpA protease, E coli (EC 3.4.21.53) ; ClpP protease, E coli (EC 3.4.21.92) ; Endopeptidase Clp (EC 3.4.21.92) ; DNA Helicases (EC 3.6.4.-) |
Sprache | Englisch |
Erscheinungsdatum | 2020-04-20 |
Erscheinungsland | United States |
Dokumenttyp | 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. ; Video-Audio Media |
ZDB-ID | 2126708-X |
ISSN | 1545-9985 ; 1545-9993 |
ISSN (online) | 1545-9985 |
ISSN | 1545-9993 |
DOI | 10.1038/s41594-020-0409-5 |
Datenquelle | MEDical Literature Analysis and Retrieval System OnLINE |
Zusatzmaterialien
Kategorien
Verfügbar in ZB MED Köln/Königswinter
Zs.A 4101: Hefte anzeigen | Standort: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG) |
|||
Zs.MG 56: Hefte anzeigen |
Über subito bestellen
Dieser Service ist kostenpflichtig (siehe Lieferbedingungen von subito). Bestellungen, die einen Artikel nebst Supplementary Material umfassen, werden grundsätzlich wie mehrfache Bestellungen bearbeitet. Gebühren fallen in diesen Fällen für jede einzelne Bestellung an.