1IZ7

Re-refinement of the structure of hydrolytic haloalkane dehalogenase linb from sphingomonas paucimobilis UT26 AT 1.6 A resolution

1IZ7 の概要

• エントリーDOI: 10.2210/pdb1iz7/pdb
• 関連するPDBエントリー: 1CV2 1D07 1IZ8 1K5P 1K63 1K6E
• 分子名称: HALOALKANE DEHALOGENASE, LINB, CHLORIDE ION, CALCIUM ION, ... (4 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: 33169.10

構造登録者

Streltsov, V.A. (登録日: 2002-09-30, 公開日: 2002-10-16, 最終更新日: 2023-12-27)

主引用文献

Streltsov, V.A.,Prokop, Z.,Damborsky, J.,Nagata, Y.,Oakley, A.,Wilce, M.C.J.
Haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26: X-ray crystallographic studies of dehalogenation of brominated substrates
Biochemistry, 42:10104-10112, 2003

PubMed Abstract: The haloalkane dehalogenases are detoxifying enzymes that convert a broad range of halogenated substrates to the corresponding alcohols. Complete crystal structures of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 (LinB), and complexes of LinB with 1,2-propanediol/1-bromopropane-2-ol and 2-bromo-2-propene-1-ol, products of debromination of 1,2-dibromopropane and 2,3-dibromopropene, respectively, were determined from 1.8 A resolution X-ray diffraction data. Published structures of native LinB and its complex with 1,3-propanediol [Marek et al. (2000) Biochemistry 39, 14082-14086] were reexamined. The full and partial debromination of 1,2-dibromopropane and 2,3-dibromopropene, respectively, conformed to the observed general trend that the sp(3)-hybridized carbon is the predominant electrophilic site for the S(N)2 bimolecular nucleophilic substitution in dehalogenation reaction. The 2-bromo-2-propene-1-ol product of 2,3-dibromopropene dehalogenation in crystal was positively identified by the gas chromatography-mass spectroscopy (GC-MS) technique. The 1,2-propanediol and 1-bromopropane-2-ol products of 1,2-dibromopropane dehalogenation in crystal were also supported by the GC-MS identification. Comparison of native LinB with its complexes showed high flexibility of residues 136-157, in particular, Asp146 and Glu147, from the cap domain helices alpha(4) and alpha(5)('). Those residues were shifted mainly in direction toward the ligand molecules in the complex structures. It seems the cap domain moves nearer to the core squeezing substrate into the active center closer to the catalytic triad. This also leads to slight contraction of the whole complex structures. The flexibility detected by crystallographic analysis is in remarkable agreement with flexibility observed by molecular dynamic simulations.

PubMed: 12939138
DOI: 10.1021/bi027280a

実験手法

X-RAY DIFFRACTION (1.58 Å)