2QO0: Crystal Structure Of The Complex Between The A246f Mutant Of Mycobacterium Beta-ketoacyl-acyl Carrier Protein Synthase Iii (fabh) And 11-(decyldithiocarbonyloxy)-undecanoic Acid

Citation:
Abstract
Mycobacterium tuberculosis FabH initiates type II fatty acid synthase-catalyzed formation of the long chain (C(16)-C(22)) acyl-coenzyme A (CoA) precursors of mycolic acids, which are major constituents of the bacterial cell envelope. Crystal structures of M. tuberculosis FabH (mtFabH) show the substrate binding site to be a buried, extended L-shaped channel with only a single solvent access portal. Entrance of an acyl-CoA substrate through the solvent portal would require energetically unfavorable reptational threading of the substrate to its reactive position. Using a class of FabH inhibitors, we have tested an alternative hypothesis that FabH exists in an "open" form during substrate binding and product release, and a "closed" form in which catalysis and intermediate steps occur. This hypothesis is supported by mass spectrometric analysis of the product profile and crystal structures of complexes of mtFabH with these inhibitors.
PDB ID: 2QO0Download
MMDB ID: 64259
PDB Deposition Date: 2007/7/19
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 1.85  Å
Source Organism:
Similar Structures:
Biological Unit for 2QO0: dimeric; determined by author and by software (PISA)
Molecular Components in 2QO0
Label Count Molecule
Proteins (2 molecules)
2
3-oxoacyl-[acyl-carrier-protein] Synthase 3
Molecule annotation
Chemicals (2 molecules)
1
2
* Click molecule labels to explore molecular sequence information.

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