2j5s
From Proteopedia
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STRUCTURAL OF ABDH, A BETA-DIKETONE HYDROLASE FROM THE CYANOBACTERIUM ANABAENA SP. PCC 7120 BOUND TO (S)-3-OXOCYCLOHEXYL ACETIC ACID
Overview
The gene alr4455 from the well-studied cyanobacterium Anabaena sp. PCC, 7120 encodes a crotonase orthologue that displays beta-diketone hydrolase, activity. Anabaena beta-diketone hydrolase (ABDH), in common with, 6-oxocamphor hydrolase (OCH) from Rhodococcus sp. NCIMB 9784, catalyzes, the desymmetrization of bicyclo[2.2.2]octane-2,6-dione to yield, [(S)-3-oxocyclohexyl]acetic acid, a reaction unusual among the crotonase, superfamily as the substrate is not an acyl-CoA thioester. The structure, of ABDH has been determined to a resolution of 1.5 A in both native and, ligand-bound forms. ABDH forms a hexamer similar to OCH and features one, active site per enzyme monomer. The arrangement of side chains in the, active site indicates that while the catalytic chemistry may be conserved, in OCH ... [(full description)]
About this Structure
2J5S is a [Single protein] structure of sequence from [Anabaena sp.] with NI and KTA as [ligands]. Active as [[1]], with EC number [3.7.1.7]. Full crystallographic information is available from [OCA].
Reference
Structural characterization of a beta-diketone hydrolase from the cyanobacterium Anabaena sp. PCC 7120 in native and product-bound forms, a coenzyme A-independent member of the crotonase suprafamily., Bennett JP, Whittingham JL, Brzozowski AM, Leonard PM, Grogan G, Biochemistry. 2007 Jan 9;46(1):137-44. PMID:17198383
Page seeded by OCA on Mon Oct 29 18:04:28 2007
