National Center for
4XTJ: N-terminal 43 Kda Fragment Of The E. Coli Dna Gyrase B Subunit Grown From 100 Mm Kcl Plus 100 Mm Nacl Condition
Acta Crystallogr. D Biol. Crystallogr. (2015) 71 p.996-1005
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 alpha-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.