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Structure paper

TitleStructural basis of rifampin inactivation by rifampin phosphotransferase
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 113, Page 3803-3808, Year 2016
Publish dateJan 28, 2016 (structure data deposition date)
AuthorsQi, X. / Lin, W. / Ma, M. / Wang, C. / He, Y. / He, N. / Gao, J. / Zhou, H. / Xiao, Y. / Wang, Y. / Zhang, P.
External linksProc. Natl. Acad. Sci. USA / PubMed:27001859
MethodsX-ray diffraction
Resolution2.912 - 3.118 Å
Structure data

PDB-5hv1:
Rifampin phosphotransferase in complex with AMPPNP and rifampin from Listeria monocytogenes
Method: X-RAY DIFFRACTION / Resolution: 3.103 Å

PDB-5hv2:
Rifampin phosphotransferase G527Y mutant from Listeria monocytogenes
Method: X-RAY DIFFRACTION / Resolution: 2.912 Å

PDB-5hv3:
Rifampin phosphotransferase G527Y mutant in complex with AMPPNP from Listeria monocytogenes
Method: X-RAY DIFFRACTION / Resolution: 3.118 Å

PDB-5hv6:
The ATP binding domain of rifampin phosphotransferase from Listeria monocytogenes
Method: X-RAY DIFFRACTION / Resolution: 3.005 Å

Chemicals

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

ChemComp-RFP:
RIFAMPICIN / antibiotic*YM

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • listeria monocytogenes (bacteria)
KeywordsTRANSFERASE / Antibiotic resistance / Rifampin / Phosphotransferase

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