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2e77
From Proteopedia
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| - | [[Image:2e77.jpg|left|200px]] | + | [[Image:2e77.jpg|left|200px]] |
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| - | '''Crystal structure of L-lactate oxidase with pyruvate complex''' | + | {{Structure |
| + | |PDB= 2e77 |SIZE=350|CAPTION= <scene name='initialview01'>2e77</scene>, resolution 1.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene> and <scene name='pdbligand=PYR:PYRUVIC ACID'>PYR</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Lactate_2-monooxygenase Lactate 2-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.12.4 1.13.12.4] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of L-lactate oxidase with pyruvate complex''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2E77 is a [ | + | 2E77 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aerococcus_viridans Aerococcus viridans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E77 OCA]. |
==Reference== | ==Reference== | ||
| - | Crystallographic study on the interaction of L-lactate oxidase with pyruvate at 1.9 Angstrom resolution., Li SJ, Umena Y, Yorita K, Matsuoka T, Kita A, Fukui K, Morimoto Y, Biochem Biophys Res Commun. 2007 Jul 13;358(4):1002-7. Epub 2007 May 11. PMID:[http:// | + | Crystallographic study on the interaction of L-lactate oxidase with pyruvate at 1.9 Angstrom resolution., Li SJ, Umena Y, Yorita K, Matsuoka T, Kita A, Fukui K, Morimoto Y, Biochem Biophys Res Commun. 2007 Jul 13;358(4):1002-7. Epub 2007 May 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17517371 17517371] |
[[Category: Aerococcus viridans]] | [[Category: Aerococcus viridans]] | ||
[[Category: Lactate 2-monooxygenase]] | [[Category: Lactate 2-monooxygenase]] | ||
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[[Category: tim barrel]] | [[Category: tim barrel]] | ||
| - | ''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 16:36:14 2008'' |
Revision as of 14:36, 20 March 2008
| |||||||
| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Lactate 2-monooxygenase, with EC number 1.13.12.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of L-lactate oxidase with pyruvate complex
Overview
L-Lactate oxidase (LOX) from Aerococcus viridans catalyzes the oxidation of L-lactate to pyruvate by the molecular oxygen and belongs to a large family of 2-hydroxy acid-dependent flavoenzymes. To investigate the interaction of LOX with pyruvate in structural details and understand the chemical mechanism of flavin-dependent L-lactate dehydrogenation, the LOX-pyruvate complex was crystallized and the crystal structure of the complex has been solved at a resolution of 1.90 Angstrom. One pyruvate molecule bound to the active site and located near N5 position of FMN for subunits, A, B, and D in the asymmetric unit, were identified. The pyruvate molecule is stabilized by the interaction of its carboxylate group with the side-chain atoms of Tyr40, Arg181, His265, and Arg268, and of its keto-oxygen atom with the side-chain atoms of Tyr146, Tyr215, and His265. The alpha-carbon of pyruvate is found to be 3.13 Angstrom from the N5 atom of FMN at an angle of 105.4 degrees from the flavin N5-N10 axis.
About this Structure
2E77 is a Single protein structure of sequence from Aerococcus viridans. Full crystallographic information is available from OCA.
Reference
Crystallographic study on the interaction of L-lactate oxidase with pyruvate at 1.9 Angstrom resolution., Li SJ, Umena Y, Yorita K, Matsuoka T, Kita A, Fukui K, Morimoto Y, Biochem Biophys Res Commun. 2007 Jul 13;358(4):1002-7. Epub 2007 May 11. PMID:17517371
Page seeded by OCA on Thu Mar 20 16:36:14 2008
