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Structure paper

TitleMycobacterium Tuberculosis DNA Gyrase ATPase Domain Structures Suggest a Dissociative Mechanism that Explains How ATP Hydrolysis is Coupled to Domain Motion.
Journal, issue, pagesBiochem. J., Vol. 456, Page 263-, Year 2013
Publish dateJan 22, 2013 (structure data deposition date)
AuthorsAgrawal, A. / Roue, M. / Spitzfaden, C. / Petrella, S. / Aubry, A. / Hann, M.M. / Bax, B. / Mayer, C.
External linksBiochem. J. / PubMed:24015710
MethodsX-ray diffraction
Resolution2.9 - 3.3 Å
Structure data

PDB-3zkb:
CRYSTAL STRUCTURE OF THE ATPASE REGION OF Mycobacterium tuberculosis GyrB WITH AMPPNP
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

PDB-3zkd:
CRYSTAL STRUCTURE OF THE ATPASE REGION OF Mycobacterium tuberculosis GyrB WITH AMPPNP
Method: X-RAY DIFFRACTION / Resolution: 2.95 Å

PDB-3zm7:
CRYSTAL STRUCTURE OF THE ATPASE REGION OF Mycobacterium tuberculosis GyrB WITH AMPPCP
Method: X-RAY DIFFRACTION / Resolution: 3.3 Å

Chemicals

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

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-ACP:
PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / AMP-PCP, energy-carrying molecule analogue*YM

Source
  • mycobacterium tuberculosis (bacteria)
KeywordsISOMERASE / TYPE IIA TOPOISOMERASE / GHKL DOMAIN

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