4FPI

Crystal Structure of 5-chloromuconolactone isomerase from Rhodococcus opacus 1CP

4FPI の概要

• エントリーDOI: 10.2210/pdb4fpi/pdb
• 分子名称: 5-chloromuconolactone dehalogenase (2 entities in total)
• 機能のキーワード: isomerase, intramolecular oxidoreductase
• 由来する生物種: Rhodococcus opacus
• タンパク質・核酸の鎖数: 20
• 化学式量合計: 224013.60

構造登録者

Ferraroni, M.,Kolomytseva, M.,Briganti, F.,Golovleva, L.A.,Scozzafava, A. (登録日: 2012-06-22, 公開日: 2013-04-24, 最終更新日: 2024-02-28)

主引用文献

Ferraroni, M.,Kolomytseva, M.,Golovleva, L.A.,Scozzafava, A.
X-ray crystallographic and molecular docking studies on a unique chloromuconolactone dehalogenase from Rhodococcus opacus 1CP.
J.Struct.Biol., 182:44-50, 2013

PubMed Abstract: 5-Chloromuconolactone dehalogenase (5-CMLD) is a unique enzyme that catalyzes the conversion of 5-chloromuconolactone into cis-dienelactone in the new modified ortho-pathway of the 3-chlorocatechol degradation by Rhodococcus opacus 1CP. In all other known chlorocatechol pathways the dehalogenation is a spontaneous secondary reaction of the unstable chloromuconate intermediate following the lactonization process catalyzed by the muconate cycloisomerases. The crystallographic structure of the decameric 5-CMLD was solved by Molecular Replacement, using the coordinates of the low resolution structure of the highly homologous muconolactone isomerase, an enzyme of the conventional ortho-pathway. Muconolactone isomerase catalyzes the endocyclic rearrangement of the double bond within the lactone ring of muconolactone to yield 3-oxoadipate enol lactone. Although both 5-CMLD and muconolactone isomerase share the ability to dechlorinate 5-chloromuconolactone, 5-CMLD shows a significant degree of specialization, having lost the capacity to convert its original substrate muconolactone. The active site of 5-CMLD was previously hypothesized to reside in a deep pocket at the interface of two different subunits, on the basis of a muconolactone isomerase structure analysis. In this study we also performed molecular docking calculations that confirmed these previous findings, and allowed us furthermore to determine the residues involved in the catalytic process.

PubMed: 23376735
DOI: 10.1016/j.jsb.2013.01.006

実験手法

X-RAY DIFFRACTION (2.2 Å)