2e77
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2e77 |SIZE=350|CAPTION= <scene name='initialview01'>2e77</scene>, resolution 1.90Å | |PDB= 2e77 |SIZE=350|CAPTION= <scene name='initialview01'>2e77</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene> | + | |LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2du2|2DU2]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e77 OCA], [http://www.ebi.ac.uk/pdbsum/2e77 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2e77 RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Morimoto, Y.]] | [[Category: Morimoto, Y.]] | ||
| - | [[Category: FMN]] | ||
| - | [[Category: PYR]] | ||
[[Category: fmn]] | [[Category: fmn]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
[[Category: tim barrel]] | [[Category: tim barrel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:44:45 2008'' |
Revision as of 23:44, 30 March 2008
| |||||||
| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Lactate 2-monooxygenase, with EC number 1.13.12.4 | ||||||
| Related: | 2DU2
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Mon Mar 31 02:44:45 2008
