4AY0

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

4AY0 の概要

• エントリーDOI: 10.2210/pdb4ay0/pdb
• 関連するPDBエントリー: 1P5U 1P5V 1Z9S 4AYF 4AZ8 4B0E 4B0M
• 分子名称: CHAPERONE PROTEIN CAF1M (2 entities in total)
• 機能のキーワード: chaperone, amino acid motifs, bacterial capsules, bacterial proteins, gene expression regulation, molecular chaperones, protein binding, protein conformation
• 由来する生物種: YERSINIA PESTIS
• 細胞内の位置: Periplasm: P26926
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48841.82

構造登録者

Yu, X.D.,Dubnovitsky, A.,Pudney, A.F.,MacIntyre, S.,Knight, S.D.,Zavialov, A.V. (登録日: 2012-06-16, 公開日: 2012-09-26, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.52 Å)