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1nu5

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{{STRUCTURE_1nu5| PDB=1nu5 | SCENE= }}
{{STRUCTURE_1nu5| PDB=1nu5 | SCENE= }}
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'''Crystal structure of Pseudomonas sp. P51 Chloromuconate lactonizing enzyme'''
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===Crystal structure of Pseudomonas sp. P51 Chloromuconate lactonizing enzyme===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12930985 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12930985}}
==About this Structure==
==About this Structure==
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[[Category: Enzyme]]
[[Category: Enzyme]]
[[Category: Muconate]]
[[Category: Muconate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:02:35 2008''

Revision as of 05:02, 28 July 2008

Image:1nu5.png

Template:STRUCTURE 1nu5

Crystal structure of Pseudomonas sp. P51 Chloromuconate lactonizing enzyme

Template:ABSTRACT PUBMED 12930985

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

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