Ontology highlight
ABSTRACT:
SUBMITTER: Hearnshaw SJ
PROVIDER: S-EPMC4388272 | biostudies-literature | 2015 Apr
REPOSITORIES: biostudies-literature
Acta crystallographica. Section D, Biological crystallography 20150327 Pt 4
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 th ...[more]