4ayf

Crystal structure of the complex of the Caf1M:Caf1 chaperone:subunit preassembly complex carrying the Tyr40Ala mutation in the Caf1M chaperone

spinqualitylabelsall models 4ayf, resolution 2.07Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ayf is a 2 chain structure with sequence from Yersinia pestis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1p5u, 1p5v, 1z9s, 4ay0, 4az8, 4b0e, 4b0m Resources: FirstGlance, OCA, RCSB, PDBsum Function [CAF1M_YERPE] Has a stimulatory role for the envelope antigen F1 secretion. It seems to interact with the subunit polypeptide and to prevent it from digestion by a protease. Publication Abstract from PubMed 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. Allosteric Mechanism Controls Traffic in the Chaperone/Usher Pathway.,Di Yu X, Dubnovitsky A, Pudney AF, Macintyre S, Knight SD, Zavialov AV Structure. 2012 Sep 11. pii: S0969-2126(12)00298-5. doi:, 10.1016/j.str.2012.08.016. PMID:22981947 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA