3ZRI

N-domain of ClpV from Vibrio cholerae

3ZRI の概要

• エントリーDOI: 10.2210/pdb3zri/pdb
• 関連するPDBエントリー: 3ZRJ
• 分子名称: CLPB PROTEIN (2 entities in total)
• 機能のキーワード: chaperone, hsp100 proteins, aaa+ proteins, t6ss, secretion, virulence
• 由来する生物種: VIBRIO CHOLERAE
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19435.87

構造登録者

Lenherr, E.D.,Kopp, J.,Sinning, I. (登録日: 2011-06-16, 公開日: 2011-06-29, 最終更新日: 2024-10-23)

主引用文献

Pietrosiuk, A.,Lenherr, E.D.,Falk, S.,Bonemann, G.,Kopp, J.,Zentgraf, H.,Sinning, I.,Mogk, A.
Molecular Basis for the Unique Role of the Aaa+ Chaperone Clpv in Type Vi Protein Secretion.
J.Biol.Chem., 286:30010-, 2011

PubMed Abstract: Ring-forming AAA(+) ATPases act in a plethora of cellular processes by remodeling macromolecules. The specificity of individual AAA(+) proteins is achieved by direct or adaptor-mediated association with substrates via distinct recognition domains. We investigated the molecular basis of substrate interaction for Vibrio cholerae ClpV, which disassembles tubular VipA/VipB complexes, an essential step of type VI protein secretion and bacterial virulence. We identified the ClpV recognition site within VipB, showed that productive ClpV-VipB interaction requires the oligomeric state of both proteins, solved the crystal structure of a ClpV N-domain-VipB peptide complex, and verified the interaction surface by mutant analysis. Our results show that the substrate is bound to a hydrophobic groove, which is formed by the addition of a single α-helix to the core N-domain. This helix is absent from homologous N-domains, explaining the unique substrate specificity of ClpV. A limited interaction surface between both proteins accounts for the dramatic increase in binding affinity upon ATP-driven ClpV hexamerization and VipA/VipB tubule assembly by coupling multiple weak interactions. This principle ensures ClpV selectivity toward the VipA/VipB macromolecular complex.

PubMed: 21733841
DOI: 10.1074/JBC.M111.253377

実験手法

X-RAY DIFFRACTION (1.8 Å)