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- Title
Crystal structure and catalytic mechanism of chloromuconolactone dehalogenase ClcF from Rhodococcus opacus 1 CP.
- Authors
Roth, Christian; Gröning, Janosch Alexander D.; Kaschabek, Stefan Rudolf; Schlömann, Michael; Sträter, Norbert
- Abstract
The actinobacterium Rhodococcus opacus 1 CP possesses a so far unique variant of the modified 3-oxoadipate pathway for 3-chlorocatechol degradation. One important feature is the novel dehalogenase ClcF, which converts (4 R,5 S)-5-chloromuconolactone to E-dienelactone. ClcF is related to muconolactone isomerase ( MLI, EC 5.3.3.4). The enzyme has a ferredoxin-type fold and forms a homodecamer of 52-symmetry, typical for the MLI family. The active site is formed by residues from two monomers. The complex structure of an E27 A variant with bound substrate in conjunction with mutational studies indicate that E27 acts as the proton acceptor in a univalent single-base syn-dehydrohalogenation mechanism. Despite the evolutionary specialization of ClcF, the conserved active-site structures suggest that the proposed mechanism is representative for the MLI family. Furthermore, ClcF represents a novel type of dehalogenase based on an isomerase scaffold.
- Subjects
CRYSTAL structure; CATALYTIC activity; DEHALOGENASES; RHODOCOCCUS; ISOMERASES
- Publication
Molecular Microbiology, 2013, Vol 88, Issue 2, p254
- ISSN
0950-382X
- Publication type
Article
- DOI
10.1111/mmi.12182