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Structure paper

TitleStructural basis for rifamycin resistance of bacterial RNA polymerase by the three most clinically important RpoB mutations found in Mycobacterium tuberculosis.
Journal, issue, pagesMol. Microbiol., Vol. 103, Page 1034-1045, Year 2017
Publish dateDec 19, 2016 (structure data deposition date)
AuthorsMolodtsov, V. / Scharf, N.T. / Stefan, M.A. / Garcia, G.A. / Murakami, K.S.
External linksMol. Microbiol. / PubMed:28009073
MethodsX-ray diffraction
Resolution3.399 - 4.1 Å
Structure data

PDB-5uac:
Escherichia coli RNA polymerase and Rifampin complex, wild-type
Method: X-RAY DIFFRACTION / Resolution: 3.8 Å

PDB-5uag:
Escherichia coli RNA polymerase mutant - RpoB D516V
Method: X-RAY DIFFRACTION / Resolution: 3.399 Å

PDB-5uah:
Escherichia coli RNA polymerase and Rifampin complex, RpoB D516V mutant
Method: X-RAY DIFFRACTION / Resolution: 4.1 Å

PDB-5uaj:
Escherichia coli RNA polymerase RpoB S531L mutant
Method: X-RAY DIFFRACTION / Resolution: 3.915 Å

PDB-5ual:
Escherichia coli RNA polymerase and Rifampin complex, RpoB S531L mutant
Method: X-RAY DIFFRACTION / Resolution: 3.887 Å

PDB-5uaq:
Escherichia coli RNA polymerase RpoB H526Y mutant
Method: X-RAY DIFFRACTION / Resolution: 3.6 Å

Chemicals

ChemComp-RFP:
RIFAMPICIN / antibiotic*YM

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

Source
  • escherichia coli (strain k12) (bacteria)
Keywordstransferase/transferase inhibitor / inhibitor / antibiotic / tuberculosis / rifampin / rifamycin / RNA polymerase / transferase-transferase inhibitor complex / rifamycin resistant mutation / rpoB-D516V / RpoB D516V mutant / RpoB S531L / TRANSFERASE / RpoB H526Y

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