1nu5
From Proteopedia
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|PDB= 1nu5 |SIZE=350|CAPTION= <scene name='initialview01'>1nu5</scene>, resolution 1.95Å | |PDB= 1nu5 |SIZE=350|CAPTION= <scene name='initialview01'>1nu5</scene>, resolution 1.95Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene> | + | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Chloromuconate_cycloisomerase Chloromuconate cycloisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.5.1.7 5.5.1.7] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Chloromuconate_cycloisomerase Chloromuconate cycloisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.5.1.7 5.5.1.7] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nu5 OCA], [http://www.ebi.ac.uk/pdbsum/1nu5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nu5 RCSB]</span> | ||
}} | }} | ||
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[[Category: Kajander, T.]] | [[Category: Kajander, T.]] | ||
[[Category: Lehtio, L.]] | [[Category: Lehtio, L.]] | ||
| - | [[Category: MN]] | ||
[[Category: dehalogenation]] | [[Category: dehalogenation]] | ||
[[Category: enzyme]] | [[Category: enzyme]] | ||
[[Category: muconate]] | [[Category: muconate]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:35:41 2008'' |
Revision as of 19:35, 30 March 2008
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| , resolution 1.95Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Chloromuconate cycloisomerase, with EC number 5.5.1.7 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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