2J5G

The Native structure of a beta-Diketone Hydrolase from the Cyanobacterium Anabaena sp. PCC 7120

2J5G の概要

• エントリーDOI: 10.2210/pdb2j5g/pdb
• 関連するPDBエントリー: 2J5J 2J5S
• 分子名称: ALR4455 PROTEIN, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: enzyme evolution, c-c bond hydrolase, hydrolase, lyase, crotonase, biocatalysis, beta-diketone
• 由来する生物種: ANABAENA SP.; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 361201.70

構造登録者

Bennett, J.P.,Whittingham, J.L.,Brzozowski, A.M.,Leonard, P.M.,Grogan, G. (登録日: 2006-09-18, 公開日: 2007-01-16, 最終更新日: 2023-12-13)

主引用文献

Bennett, J.P.,Whittingham, J.L.,Brzozowski, A.M.,Leonard, P.M.,Grogan, G.
Structural Characterisation 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
Biochemistry, 46:137-, 2007

PubMed Abstract: 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 orthologues, the structural determinants of substrate specificity are different. In the active site of ligand-bound forms that had been cocrystallized with the bicyclic diketone substrate bicyclo[2.2.2]octane-2,6-dione was found the product of the asymmetric enzymatic retro-Claisen reaction [(S)-3-oxocyclohexyl]acetic acid. The structures of ABDH in both native and ligand-bound forms reveal further details about structural variation and modes of coenzyme A-independent activity within the crotonases and provide further evidence of a wider suprafamily of enzymes that have recruited the crotonase fold for the catalysis of reactions other than those regularly attributed to canonical superfamily members.

PubMed: 17198383
DOI: 10.1021/BI061900G

実験手法

X-RAY DIFFRACTION (1.46 Å)