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

Summary for 3DPB

• Entry DOI: 10.2210/pdb3dpb/pdb
• Related: 1P5U 1Z9S 3DOS 3DSN
• Descriptor: Chaperone protein caf1M, F1 capsule antigen (3 entities in total)
• Functional Keywords: donor strand complementation, fimbriae, chaperone, protein-protein complex, beta barrel, immunoglobulin domain, periplasm, plasmid, capsule, secreted, chaperone-structural protein complex, chaperone/structural protein
• Biological source: Yersinia pestis; More
• Cellular location: Periplasm: P26926; Secreted, capsule: P26948
• Total number of polymer chains: 3
• Total formula weight: 57563.48

Authors

Fooks, L.J.,Yu, X.,Moslehi-Mohebi, E.,Tischenko, V.,Knight, S.D.,MacIntyre, S.,Zavialov, A.V. (deposition date: 2008-07-07, release date: 2009-07-14, Last modification date: 2023-08-30)

• Primary citation: Fooks, L.J.,Yu, X.,Moslehi-Mohebi, E.,Tischenko, V.,Knight, S.D.,MacIntyre, S.,Zavialov, A.V.; Hydrophobicity and rigidity of binding segments enable CAF1M chaperone to act as assembly catalyst; To be published,

Experimental method

X-RAY DIFFRACTION (2.2 Å)