5IT5
Thermus thermophilus PilB core ATPase region
Summary for 5IT5
| Entry DOI | 10.2210/pdb5it5/pdb |
| Descriptor | ATP binding motif-containing protein PilF, ZINC ION, ADENOSINE-5'-TRIPHOSPHATE, ... (6 entities in total) |
| Functional Keywords | atpase, aaa+, hexamer, type iv pilus, transport protein |
| Biological source | Thermus thermophilus |
| Total number of polymer chains | 6 |
| Total formula weight | 258726.43 |
| Authors | Mancl, J.,Robinson, H.,Black, W.,Yang, Z.,Schubot, F. (deposition date: 2016-03-16, release date: 2016-10-19, Last modification date: 2023-09-27) |
| Primary citation | Mancl, J.M.,Black, W.P.,Robinson, H.,Yang, Z.,Schubot, F.D. Crystal Structure of a Type IV Pilus Assembly ATPase: Insights into the Molecular Mechanism of PilB from Thermus thermophilus. Structure, 24:1886-1897, 2016 Cited by PubMed Abstract: Type IV pili (T4P) mediate bacterial motility and virulence. The PilB/GspE family ATPases power the assembly of T4P and type 2 secretion systems. We determined the structure of the ATPase region of PilB (PilB) in complex with ATPγS to provide a model of a T4P assembly ATPase and a view of a PilB/GspE family hexamer at better than 3-Å resolution. Spatial positioning and conformations of the protomers suggest a mechanism of force generation. All six PilB protomers contain bound ATPγS. Two protomers form a closed conformation poised for ATP hydrolysis. The other four molecules assume an open conformation but separate into two pairs with distinct active-site accessibilities. We propose that one pair represents the post-hydrolysis phase while the other pair appears poised for ADP/ATP exchange. Collectively, the data suggest that T4P assembly is powered by coordinating concurrent substrate binding with ATP hydrolysis across the PilB hexamer. PubMed: 27667690DOI: 10.1016/j.str.2016.08.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.648 Å) |
Structure validation
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