4WUC
N-terminal 43 kDa fragment of the E. coli DNA gyrase B subunit grown from 100 mM NaCl condition
Summary for 4WUC
| Entry DOI | 10.2210/pdb4wuc/pdb |
| Descriptor | DNA gyrase subunit B, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (6 entities in total) |
| Functional Keywords | dna gyrase, atpase domain, atpase activity, ghkl superfamily, monovalent cations, isomerase |
| Biological source | Escherichia coli strain K-12 |
| Cellular location | Cytoplasm : P0AES6 |
| Total number of polymer chains | 1 |
| Total formula weight | 43927.70 |
| Authors | Hearnshaw, S.J.,Chung, T.T.,Stevenson, C.E.M.,Maxwell, A.,Lawson, D.M. (deposition date: 2014-10-31, release date: 2015-04-08, Last modification date: 2024-01-10) |
| Primary citation | Hearnshaw, S.J.,Chung, T.T.,Stevenson, C.E.M.,Maxwell, A.,Lawson, D.M. The role of monovalent cations in the ATPase reaction of DNA gyrase Acta Crystallogr.,Sect.D, 71:996-1005, 2015 Cited by PubMed Abstract: Four new crystal structures of the ATPase domain of the GyrB subunit of Escherichia coli DNA gyrase have been determined. One of these, solved in the presence of K(+), is the highest resolution structure reported so far for this domain and, in conjunction with the three other structures, reveals new insights into the function of this domain. Evidence is provided for the existence of two monovalent cation-binding sites: site 1, which preferentially binds a K(+) ion that interacts directly with the α-phosphate of ATP, and site 2, which preferentially binds an Na(+) ion and the functional significance of which is not clear. The crystallographic data are corroborated by ATPase data, and the structures are compared with those of homologues to investigate the broader conservation of these sites. PubMed: 25849408DOI: 10.1107/S1399004715002916 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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