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Structure paper

TitleInhA, the enoyl-thioester reductase fromMycobacterium tuberculosisforms a covalent adduct during catalysis.
Journal, issue, pagesJ. Biol. Chem., Vol. 293, Page 17200-17207, Year 2018
Publish dateOct 11, 2017 (structure data deposition date)
AuthorsVogeli, B. / Rosenthal, R.G. / Stoffel, G.M.M. / Wagner, T. / Kiefer, P. / Cortina, N.S. / Shima, S. / Erb, T.J.
External linksJ. Biol. Chem. / PubMed:30217823
MethodsX-ray diffraction
Resolution1.8 Å
Structure data

PDB-6ep8:
InhA Y158F mutant in complex with NADH from Mycobacterium tuberculosis
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-GOL:
GLYCEROL

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

ChemComp-HOH:
WATER

Source
  • mycobacterium tuberculosis h37rv (bacteria)
KeywordsOXIDOREDUCTASE / mycolic acid biosynthetic process / therapeutic target / isoniazid / mutation / catalytic mechanism / enoyl thioester reductases / tuberculosis

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