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Structure paper

TitleHydrophobicity and rigidity of binding segments enable CAF1M chaperone to act as assembly catalyst
Journal, issue, pagesTO BE PUBLISHED
Publish dateJul 6, 2008 (structure data deposition date)
AuthorsFooks, L.J. / Yu, X. / Moslehi-Mohebi, E. / Tischenko, V. / Knight, S.D. / MacIntyre, S. / Zavialov, A.V.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution2.2 - 2.4 Å
Structure data

PDB-3dos:
Crystal structure of the complex of the Caf1M chaperone with the mini-fiber of two Caf1 subunits (Caf1:Caf1), carrying the Thr7Phe and Ala9Val mutations in the Gd donor strand
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-3dpb:
Crystal structure of the complex of the Caf1M chaperone with the mini-fiber of two Caf1 subunits (Caf1:Caf1), carrying the Ala9Val, Ala11Val, and Leu13Val mutations in the Gd donor strand
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-3dsn:
Crystal structure of the complex of the Caf1M chaperone with the mini-fiber of two Caf1 subunits (Caf1:Caf1), carrying the Thr7Phe mutation in the Gd donor strand
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • yersinia pestis (bacteria)
KeywordsChaperone/Structural Protein / BETA BARREL / PROTEIN-PROTEIN COMPLEX / DONOR STRAND COMPLEMENTATION / Chaperone / Immunoglobulin domain / Periplasm / Plasmid / Capsule / Secreted / Chaperone-Structural Protein COMPLEX / FIMBRIAE / FIMBRIAL SUBUNIT

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