1ds1
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(New page: 200px<br /><applet load="1ds1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ds1, resolution 1.08Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 11:25, 20 November 2007
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CRYSTAL STRUCTURE OF CLAVAMINATE SYNTHASE IN COMPLEX WITH FE(II) AND 2-OXOGLUTARATE
Overview
Clavaminate synthase (CAS), a remarkable Fe(II)/2-oxoglutarate oxygenase, catalyzes three separate oxidative reactions in the biosynthesis of, clavulanic acid, a clinically used inhibitor of serine beta-lactamases., The first CAS-catalyzed step (hydroxylation) is separated from the latter, two (oxidative cyclization/desaturation) by the action of an, amidinohydrolase. Here, we describe crystal structures of CAS in complex, with Fe(II), 2-oxoglutarate (2OG) and substrates, (N-alpha-acetyl-L-arginine and proclavaminic acid). They reveal how CAS, catalyzes formation of the clavam nucleus, via a process unprecedented in, synthetic organic chemistry, and suggest how it discriminates between, substrates and controls reaction of its highly reactive ferryl, intermediate. The presence of an unpredicted jelly roll beta-barrel core, in CAS implies divergent evolution within the family of 2OG and related, oxygenases. Comparison with other non-heme oxidases/oxygenases reveals, flexibility in the position which dioxygen ligates to the iron, in, contrast to the analogous heme-using enzymes.
About this Structure
1DS1 is a Single protein structure of sequence from Streptomyces clavuligerus with SO4, FE2, AKG and PGO as ligands. Full crystallographic information is available from OCA.
Reference
Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase., Zhang Z, Ren J, Stammers DK, Baldwin JE, Harlos K, Schofield CJ, Nat Struct Biol. 2000 Feb;7(2):127-33. PMID:10655615
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