5ESR

Crystal structure of haloalkane dehalogenase (DccA) from Caulobacter crescentus

5ESR の概要

• エントリーDOI: 10.2210/pdb5esr/pdb
• 分子名称: Haloalkane dehalogenase, COBALT (II) ION, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Caulobacter crescentus (strain ATCC 19089 / CB15)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34458.83

構造登録者

Malashkevich, V.N.,Toro, R.,Mundorff, E.C.,Almo, S.C. (登録日: 2015-11-17, 公開日: 2016-06-01, 最終更新日: 2023-09-27)

主引用文献

Carlucci, L.,Zhou, E.,Malashkevich, V.N.,Almo, S.C.,Mundorff, E.C.
Biochemical characterization of two haloalkane dehalogenases: DccA from Caulobacter crescentus and DsaA from Saccharomonospora azurea.
Protein Sci., 25:877-886, 2016

PubMed Abstract: Two putative haloalkane dehalogenases (HLDs) of the HLD-I subfamily, DccA from Caulobacter crescentus and DsaA from Saccharomonospora azurea, have been identified based on sequence comparisons with functionally characterized HLD enzymes. The two genes were synthesized, functionally expressed in E. coli and shown to have activity toward a panel of haloalkane substrates. DsaA has a moderate activity level and a preference for long (greater than 3 carbons) brominated substrates, but little activity toward chlorinated alkanes. DccA shows high activity with both long brominated and chlorinated alkanes. The structure of DccA was determined by X-ray crystallography and was refined to 1.5 Å resolution. The enzyme has a large and open binding pocket with two well-defined access tunnels. A structural alignment of HLD-I subfamily members suggests a possible basis for substrate specificity is due to access tunnel size.

PubMed: 26833751
DOI: 10.1002/pro.2895

実験手法

X-RAY DIFFRACTION (1.476 Å)