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Structure paper

TitleAllosteric Mechanism Controls Traffic in the Chaperone/Usher Pathway.
Journal, issue, pagesStructure, Vol. 20, Page 1861-, Year 2012
Publish dateJun 16, 2012 (structure data deposition date)
AuthorsDi Yu, X. / Dubnovitsky, A. / Pudney, A.F. / Macintyre, S. / Knight, S.D. / Zavialov, A.V.
External linksStructure / PubMed:22981947
MethodsX-ray diffraction
Resolution1.52 - 2.65 Å
Structure data

PDB-4ay0:
High resolution crystal structure of the monomeric subunit-free Caf1M chaperone
Method: X-RAY DIFFRACTION / Resolution: 1.52 Å

PDB-4ayf:
Crystal structure of the complex of the Caf1M:Caf1 chaperone:subunit preassembly complex carrying the Tyr40Ala mutation in the Caf1M chaperone
Method: X-RAY DIFFRACTION / Resolution: 2.07 Å

PDB-4az8:
Crystal structure of the complex of the Caf1M:Caf1 chaperone:subunit preassembly complex carrying the KDKDTN insertion at the F1G1 loop region
Method: X-RAY DIFFRACTION / Resolution: 2.65 Å

PDB-4b0e:
Crystal structure of the Caf1A usher protein N-terminal domain from Yersinia pestis
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-4b0m:
Complex of the Caf1AN usher domain, Caf1M chaperone and Caf1 subunit from Yersinia pestis
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • yersinia pestis (bacteria)
KeywordsCHAPERONE / AMINO ACID MOTIFS / BACTERIAL CAPSULES / BACTERIAL PROTEINS / GENE EXPRESSION REGULATION / MOLECULAR CHAPERONES / PROTEIN BINDING / PROTEIN CONFORMATION / CHAPERONE/ANTIGEN / CHAPERONE-ANTIGEN COMPLEX / ANTIGENS / FIMBRIAE / PROTEIN FOLDING / CHAPERONE/IMMUNE SYSTEM / CHAPERONE-IMMUNE SYSTEM COMPLEX / TRANSPORT PROTEIN / CHAPERONE-USHER PATHWAY / PILI ASSEMBLY / PROTEIN TRANSPORT

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