2GZA
Crystal structure of the VirB11 ATPase from the Brucella Suis type IV secretion system in complex with sulphate
Summary for 2GZA
| Entry DOI | 10.2210/pdb2gza/pdb |
| Descriptor | Type IV secretion system protein VirB11, SULFATE ION (3 entities in total) |
| Functional Keywords | secretion, atpase, hydrolase |
| Biological source | Brucella suis |
| Cellular location | Cytoplasm : Q8FXK7 |
| Total number of polymer chains | 3 |
| Total formula weight | 122626.87 |
| Authors | Hare, S.,Bayliss, R.,Baron, C.,Waksman, G. (deposition date: 2006-05-11, release date: 2006-07-11, Last modification date: 2023-08-30) |
| Primary citation | Hare, S.,Bayliss, R.,Baron, C.,Waksman, G. A Large Domain Swap in the VirB11 ATPase of Brucella suis Leaves the Hexameric Assembly Intact J.Mol.Biol., 360:56-66, 2006 Cited by PubMed Abstract: VirB11 ATPases are hexameric assemblies that power type IV secretion systems in bacteria. The hexamer of Brucella suis VirB11 (BsB11), like that of the Helicobacter pylori VirB11 (Hp0525), consists of a double ring structure formed by the N-terminal and C-terminal domains of each monomer. However, the monomer differs dramatically from that of Hp0525 by a large domain swap that leaves the hexameric assembly intact but profoundly alters the nucleotide-binding site and the interface between subunits. PubMed: 16730027DOI: 10.1016/j.jmb.2006.04.060 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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