1nu5: Difference between revisions
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'''Crystal structure of Pseudomonas sp. P51 Chloromuconate lactonizing enzyme''' | {{Structure | ||
|PDB= 1nu5 |SIZE=350|CAPTION= <scene name='initialview01'>1nu5</scene>, resolution 1.95Å | |||
|SITE= | |||
|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] | |||
|GENE= | |||
}} | |||
'''Crystal structure of Pseudomonas sp. P51 Chloromuconate lactonizing enzyme''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1NU5 is a [ | 1NU5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NU5 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12930985 12930985] | ||
[[Category: Chloromuconate cycloisomerase]] | [[Category: Chloromuconate cycloisomerase]] | ||
[[Category: Pseudomonas sp.]] | [[Category: Pseudomonas sp.]] | ||
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[[Category: muconate]] | [[Category: muconate]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:01:43 2008'' | ||
Revision as of 11:01, 20 March 2008
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| 1nu5, resolution 1.95Å | |||||||||||||
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| Ligands: | MN | ||||||||||||
| Activity: | Chloromuconate cycloisomerase, with EC number 5.5.1.7 | ||||||||||||
| 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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