4AY0

High resolution crystal structure of the monomeric subunit-free Caf1M chaperone

Summary for 4AY0

• Entry DOI: 10.2210/pdb4ay0/pdb
• Related: 1P5U 1P5V 1Z9S 4AYF 4AZ8 4B0E 4B0M
• Descriptor: CHAPERONE PROTEIN CAF1M (2 entities in total)
• Functional Keywords: chaperone, amino acid motifs, bacterial capsules, bacterial proteins, gene expression regulation, molecular chaperones, protein binding, protein conformation
• Biological source: YERSINIA PESTIS
• Cellular location: Periplasm: P26926
• Total number of polymer chains: 2
• Total formula weight: 48841.82

Authors

Yu, X.D.,Dubnovitsky, A.,Pudney, A.F.,MacIntyre, S.,Knight, S.D.,Zavialov, A.V. (deposition date: 2012-06-16, release date: 2012-09-26, Last modification date: 2023-12-20)

Primary citation

Di Yu, X.,Dubnovitsky, A.,Pudney, A.F.,Macintyre, S.,Knight, S.D.,Zavialov, A.V.
Allosteric Mechanism Controls Traffic in the Chaperone/Usher Pathway.
Structure, 20:1861-, 2012

PubMed Abstract: Many virulence organelles of Gram-negative bacterial pathogens are assembled via the chaperone/usher pathway. The chaperone transports organelle subunits across the periplasm to the outer membrane usher, where they are released and incorporated into growing fibers. Here, we elucidate the mechanism of the usher-targeting step in assembly of the Yersinia pestis F1 capsule at the atomic level. The usher interacts almost exclusively with the chaperone in the chaperone:subunit complex. In free chaperone, a pair of conserved proline residues at the beginning of the subunit-binding loop form a "proline lock" that occludes the usher-binding surface and blocks usher binding. Binding of the subunit to the chaperone rotates the proline lock away from the usher-binding surface, allowing the chaperone-subunit complex to bind to the usher. We show that the proline lock exists in other chaperone/usher systems and represents a general allosteric mechanism for selective targeting of chaperone:subunit complexes to the usher and for release and recycling of the free chaperone.

PubMed: 22981947
DOI: 10.1016/J.STR.2012.08.016

Experimental method

X-RAY DIFFRACTION (1.52 Å)