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1nu5
From Proteopedia
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'''Crystal structure of Pseudomonas sp. P51 Chloromuconate lactonizing enzyme''' | '''Crystal structure of Pseudomonas sp. P51 Chloromuconate lactonizing enzyme''' | ||
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[[Category: Kajander, T.]] | [[Category: Kajander, T.]] | ||
[[Category: Lehtio, L.]] | [[Category: Lehtio, L.]] | ||
| - | [[Category: | + | [[Category: Dehalogenation]] |
| - | [[Category: | + | [[Category: Enzyme]] |
| - | [[Category: | + | [[Category: Muconate]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:58:54 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 23:58, 2 May 2008
Crystal structure of Pseudomonas sp. P51 Chloromuconate lactonizing enzyme
Overview
Bacterial muconate lactonizing enzymes (MLEs) catalyze the conversion of cis,cis-muconate as a part of the beta-ketoadipate pathway, and some MLEs are also able to dehalogenate chlorinated muconates (Cl-MLEs). The basis for the Cl-MLEs dehalogenating activity is still unclear. To further elucidate the differences between MLEs and Cl-MLEs, we have solved the structure of Pseudomonas P51 Cl-MLE at 1.95 A resolution. Comparison of Pseudomonas MLE and Cl-MLE structures reveals the presence of a large cavity in the Cl-MLEs. The cavity may be related to conformational changes on substrate binding in Cl-MLEs, at Gly52. Site-directed mutagenesis on Pseudomonas MLE core positions to the equivalent Cl-MLE residues showed that the variant Thr52Gly was rather inactive, whereas the Thr52Gly-Phe103Ser variant had regained part of the activity. These residues form a hydrogen bond in the Cl-MLEs. The Cl-MLE structure, as a result of the Thr-to-Gly change, is more flexible than MLE: As a mobile loop closes over the active site, a conformational change at Gly52 is observed in Cl-MLEs. The loose packing and structural motions in Cl-MLE may be required for the rotation of the lactone ring in the active site necessary for the dehalogenating activity of Cl-MLEs. Furthermore, we also suggest that differences in the active site mobile loop sequence between MLEs and Cl-MLEs result in lower active site polarity in Cl-MLEs, possibly affecting catalysis. These changes could result in slower product release from Cl-MLEs and make it a better enzyme for dehalogenation of substrate.
About this Structure
1NU5 is a Single protein structure of sequence from Pseudomonas sp.. Full crystallographic information is available from OCA.
Reference
The structure of Pseudomonas P51 Cl-muconate lactonizing enzyme: co-evolution of structure and dynamics with the dehalogenation function., Kajander T, Lehtio L, Schlomann M, Goldman A, Protein Sci. 2003 Sep;12(9):1855-64. PMID:12930985 Page seeded by OCA on Sat May 3 02:58:54 2008
