6OK2
PilT4 from Geobacter metallireducens bound to ADP: C3ocococ conformation
Summary for 6OK2
| Entry DOI | 10.2210/pdb6ok2/pdb |
| Related | 6OJX 6OJY 6OJZ 6OKV 6OLJ 6OLK 6OLL 6OLM |
| Descriptor | Twitching motility pilus retraction ATPase, ADENOSINE-5'-DIPHOSPHATE (3 entities in total) |
| Functional Keywords | t4p, atpase, type iv pilus, motor, motor protein |
| Biological source | Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210) |
| Total number of polymer chains | 6 |
| Total formula weight | 259863.48 |
| Authors | McCallum, M.,Howell, P.L. (deposition date: 2019-04-12, release date: 2019-11-20, Last modification date: 2023-10-11) |
| Primary citation | McCallum, M.,Benlekbir, S.,Nguyen, S.,Tammam, S.,Rubinstein, J.L.,Burrows, L.L.,Howell, P.L. Multiple conformations facilitate PilT function in the type IV pilus. Nat Commun, 10:5198-5198, 2019 Cited by PubMed Abstract: Type IV pilus-like systems are protein complexes that polymerize pilin fibres. They are critical for virulence in many bacterial pathogens. Pilin polymerization and depolymerization are powered by motor ATPases of the PilT/VirB11-like family. This family is thought to operate with C symmetry; however, most of these ATPases crystallize with either C or C symmetric conformations. The relevance of these conformations is unclear. Here, we determine the X-ray structures of PilT in four unique conformations and use these structures to classify the conformation of available PilT/VirB11-like family member structures. Single particle electron cryomicroscopy (cryoEM) structures of PilT reveal condition-dependent preferences for C C, and C conformations. The physiologic importance of these conformations is validated by coevolution analysis and functional studies of point mutants, identifying a rare gain-of-function mutation that favours the C conformation. With these data, we propose a comprehensive model of PilT function with broad implications for PilT/VirB11-like family members. PubMed: 31729381DOI: 10.1038/s41467-019-13070-z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.287 Å) |
Structure validation
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