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Structure paper

TitleThe role of monovalent cations in the ATPase reaction of DNA gyrase
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 71, Page 996-1005, Year 2015
Publish dateOct 31, 2014 (structure data deposition date)
AuthorsHearnshaw, S.J. / Chung, T.T. / Stevenson, C.E.M. / Maxwell, A. / Lawson, D.M.
External linksActa Crystallogr. ,Sect. D / PubMed:25849408
MethodsX-ray diffraction
Resolution1.75 - 1.95 Å
Structure data

PDB-4wub:
N-terminal 43 kDa fragment of the E. coli DNA gyrase B subunit grown from 100 mM KCl condition
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-4wuc:
N-terminal 43 kDa fragment of the E. coli DNA gyrase B subunit grown from 100 mM NaCl condition
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-4wud:
N-terminal 43 kDa fragment of the E. coli DNA gyrase B subunit grown from no salt condition
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-4xtj:
N-terminal 43 kDa fragment of the E. coli DNA gyrase B subunit grown from 100 mM KCl plus 100 mM NaCl condition
Method: X-RAY DIFFRACTION / Resolution: 1.92 Å

Chemicals

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-K:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • escherichia coli (strain k12) (bacteria)
  • escherichia coli strain k-12 (bacteria)
KeywordsISOMERASE / DNA gyrase / ATPase domain / ATPase activity / GHKL superfamily / monovalent cations

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