1CV2

Hydrolytic haloalkane dehalogenase linb from sphingomonas paucimobilis UT26 AT 1.6 A resolution

1CV2 の概要

• エントリーDOI: 10.2210/pdb1cv2/pdb
• 分子名称: HALOALKANE DEHALOGENASE (2 entities in total)
• 機能のキーワード: dehalogenase, lindane, biodegradation, alpha/beta-hydrolase, hydrolase
• 由来する生物種: Sphingomonas paucimobilis
• 細胞内の位置: Periplasm : P51698
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33144.61

構造登録者

Marek, J.,Vevodova, J.,Damborsky, J.,Smatanova, I.,Svensson, L.A.,Newman, J.,Nagata, Y.,Takagi, M. (登録日: 1999-08-22, 公開日: 2000-09-11, 最終更新日: 2023-08-09)

主引用文献

Marek, J.,Vevodova, J.,Smatanova, I.K.,Nagata, Y.,Svensson, L.A.,Newman, J.,Takagi, M.,Damborsky, J.
Crystal structure of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26.
Biochemistry, 39:14082-14086, 2000

PubMed Abstract: The haloalkane dehalogenase from Sphingomonas paucimobilis UT26 (LinB) is the enzyme involved in the degradation of the important environmental pollutant gamma-hexachlorocyclohexane. The enzyme hydrolyzes a broad range of halogenated cyclic and aliphatic compounds. Here, we present the 1.58 A crystal structure of LinB and the 2.0 A structure of LinB with 1,3-propanediol, a product of debromination of 1,3-dibromopropane, in the active site of the enzyme. The enzyme belongs to the alpha/beta hydrolase family and contains a catalytic triad (Asp108, His272, and Glu132) in the lipase-like topological arrangement previously proposed from mutagenesis experiments. The LinB structure was compared with the structures of haloalkane dehalogenase from Xanthobacter autotrophicus GJ10 and from Rhodococcus sp. and the structural features involved in the adaptation toward xenobiotic substrates were identified. The arrangement and composition of the alpha-helices in the cap domain results in the differences in the size and shape of the active-site cavity and the entrance tunnel. This is the major determinant of the substrate specificity of this haloalkane dehalogenase.

PubMed: 11087355
DOI: 10.1021/bi001539c

実験手法

X-RAY DIFFRACTION (1.58 Å)