3JVV
Crystal Structure of P. aeruginosa PilT with bound AMP-PCP
Summary for 3JVV
| Entry DOI | 10.2210/pdb3jvv/pdb |
| Related | 2ewv 2eww 2gsz 3jvu |
| Descriptor | Twitching mobility protein, PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | hexameric p-loop atpase, secretion atpase, atp-binding, fimbrium, nucleotide-binding, transport, atp binding protein |
| Biological source | Pseudomonas aeruginosa |
| Cellular location | Cytoplasm (Probable): P24559 |
| Total number of polymer chains | 3 |
| Total formula weight | 120023.65 |
| Authors | Misic, A.M.,Satyshur, K.A.,Forest, K.T. (deposition date: 2009-09-17, release date: 2010-06-02, Last modification date: 2023-09-06) |
| Primary citation | Misic, A.M.,Satyshur, K.A.,Forest, K.T. P. aeruginosa PilT structures with and without nucleotide reveal a dynamic type IV pilus retraction motor. J.Mol.Biol., 400:1011-1021, 2010 Cited by PubMed Abstract: Type IV pili are bacterial extracellular filaments that can be retracted to create force and motility. Retraction is accomplished by the motor protein PilT. Crystal structures of Pseudomonas aeruginosa PilT with and without bound beta,gamma-methyleneadenosine-5'-triphosphate have been solved at 2.6 A and 3.1 A resolution, respectively, revealing an interlocking hexamer formed by the action of a crystallographic 2-fold symmetry operator on three subunits in the asymmetric unit and held together by extensive ionic interactions. The roles of two invariant carboxylates, Asp Box motif Glu163 and Walker B motif Glu204, have been assigned to Mg(2+) binding and catalysis, respectively. The nucleotide ligands in each of the subunits in the asymmetric unit of the beta,gamma-methyleneadenosine-5'-triphosphate-bound PilT are not equally well ordered. Similarly, the three subunits in the asymmetric unit of both structures exhibit differing relative conformations of the two domains. The 12 degrees and 20 degrees domain rotations indicate motions that occur during the ATP-coupled mechanism of the disassembly of pili into membrane-localized pilin monomers. Integrating these observations, we propose a three-state "Ready, Active, Release" model for the action of PilT. PubMed: 20595000DOI: 10.1016/j.jmb.2010.05.066 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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