3ZRJ
Complex of ClpV N-domain with VipB peptide
Summary for 3ZRJ
| Entry DOI | 10.2210/pdb3zrj/pdb |
| Related | 3ZRI |
| Descriptor | CLPB PROTEIN, VIPB, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | chaperone-peptide complex, hsp100 proteins, aaa+ proteins, t6ss, secretion, virulence, chaperone/peptide |
| Biological source | VIBRIO CHOLERAE More |
| Total number of polymer chains | 4 |
| Total formula weight | 43425.83 |
| Authors | Lenherr, E.D.,Kopp, J.,Sinning, I. (deposition date: 2011-06-16, release date: 2011-07-06, Last modification date: 2024-11-13) |
| Primary citation | 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 Cited by 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: 21733841DOI: 10.1074/JBC.M111.253377 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.94 Å) |
Structure validation
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