4XTJ

N-terminal 43 kDa fragment of the E. coli DNA gyrase B subunit grown from 100 mM KCl plus 100 mM NaCl condition

4XTJ の概要

• エントリーDOI: 10.2210/pdb4xtj/pdb
• 分子名称: DNA gyrase subunit B, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (7 entities in total)
• 機能のキーワード: dna gyrase, atpase domain, atpase activity, ghkl superfamily, monovalent cations, isomerase
• 由来する生物種: Escherichia coli (strain K12)
• 細胞内の位置: Cytoplasm : P0AES6
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43786.61

構造登録者

Hearnshaw, S.J.,Chung, T.T.,Stevenson, C.E.M.,Maxwell, A.,Lawson, D.M. (登録日: 2015-01-23, 公開日: 2015-04-08, 最終更新日: 2024-01-10)

主引用文献

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

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: 25849408
DOI: 10.1107/S1399004715002916

実験手法

X-RAY DIFFRACTION (1.92 Å)