2fa0

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spinqualitylabelsall models PDB ID 2fa0 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 2.49Å
Ligands:
Coordinates:	save as pdb, mmCIF, xml

HMG-CoA synthase from Brassica juncea in complex with HMG-CoA and covalently bound to HMG-CoA

Overview

3-Hydroxy-3-methylglutaryl CoA synthase (HMGS) catalyzes the first committed step in the mevalonate metabolic pathway for isoprenoid biosynthesis and serves as an alternative target for cholesterol-lowering and antibiotic drugs. We have determined a previously undescribed crystal structure of a eukaryotic HMGS bound covalently to a potent and specific inhibitor F-244 [(E,E)-11-[3-(hydroxymethyl)-4-oxo-2-oxytanyl]-3,5,7-trimethyl-2,4-undecad ienenoic acid]. Given the accessibility of synthetic analogs of the F-244 natural product, this inhibited eukaryotic HMGS structure serves as a necessary starting point for structure-based methods that may improve the potency and species-specific selectivity of the next generation of F-244 analogs designed to target particular eukaryotic and prokaryotic HMGS.

About this Structure

2FA0 is a Single protein structure of sequence from Brassica juncea. Full crystallographic information is available from OCA.

Reference

Structural basis for the design of potent and species-specific inhibitors of 3-hydroxy-3-methylglutaryl CoA synthases., Pojer F, Ferrer JL, Richard SB, Nagegowda DA, Chye ML, Bach TJ, Noel JP, Proc Natl Acad Sci U S A. 2006 Aug 1;103(31):11491-6. Epub 2006 Jul 24. PMID:16864776

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