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The role of monovalent cations in the ATPase reaction of DNA gyrase

DOI: 10.1107/S1399004715002916 DOI Help
PMID: 25849408 PMID Help

Authors: Stephen Hearnshaw (John Innes Centre) , Terence Chung (John Innes Centre) , Clare Stevenson (John Innes Centre) , Anthony Maxwell (John Innes Centre) , David Lawson (John Innes Centre)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section D , VOL 71 , PAGES 996-1005

State: Published (Approved)
Published: February 2015
Diamond Proposal Number(s): 1219 , 7641

Open Access Open Access

Abstract: Abstract We have determined four new crystal structures of the ATPase domain of the GyrB subunit of Escherichia coli DNA gyrase. 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. We show evidence for the existence of two monovalent cation-binding sites: site 1, which preferentially binds a K+ ion that interacts directly with the Ą-phosphate of ATP, and site 2, which preferentially binds a Na+ ion, whose functional significance is not clear. The crystallographic data are corroborated by ATPase data, and we compare our structures with those of homologues to investigate the broader conservation of these sites.

Journal Keywords: Dna Gyrase; Atpase Domain; Atpase Activity; Ghkl Superfamily; Monovalent Cations

Subject Areas: Biology and Bio-materials, Medicine

Instruments: I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography , I24-Microfocus Macromolecular Crystallography

Added On: 20/03/2015 11:31


Discipline Tags:

Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)