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TitleProbing reactivity and substrate specificity of both subunits of the dimeric Mycobacterium tuberculosis FabH using alkyl-CoA disulfide inhibitors and acyl-CoA substrates
Journal, issue, pagesBioorg. Chem., Vol. 36, Page 85-90, Year 2008
Publish dateAug 10, 2007 (structure data deposition date)
AuthorsSachdeva, S. / Musayev, F. / Alhamadsheh, M.M. / Neel Scarsdale, J. / Tonie Wright, H. / Reynolds, K.A.
External linksBioorg. Chem. / PubMed:18096200
MethodsX-ray diffraction
Resolution2.6 Å
Structure data

PDB-2qx1:
Crystal structure of the complex between mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III (FABH) and decyl-COA disulfide
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-COA:
COENZYME A

ChemComp-D1T:
DECANE-1-THIOL

ChemComp-HOH:
WATER

Source
  • mycobacterium tuberculosis (bacteria)
KeywordsTRANSFERASE / FATTY ACID BIOSYNTHESIS / MYOBACTERIUM TUBERCULOSIS / STRUCTURAL BASIS FOR SUBSTRATE SPECIFICITY / ENZYME INHIBITOR COMPLEX / MECHANISM BASED INHIBITOR / Acyltransferase / Lipid synthesis / Multifunctional enzyme

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