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2e77

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[[Image:2e77.jpg|left|200px]]
[[Image:2e77.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2e77 |SIZE=350|CAPTION= <scene name='initialview01'>2e77</scene>, resolution 1.90&Aring;
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The line below this paragraph, containing "STRUCTURE_2e77", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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{{STRUCTURE_2e77| PDB=2e77 | SCENE= }}
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|RELATEDENTRY=[[2du2|2DU2]]
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|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>
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'''Crystal structure of L-lactate oxidase with pyruvate complex'''
'''Crystal structure of L-lactate oxidase with pyruvate complex'''
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[[Category: Single protein]]
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[[Category: Morimoto, Y.]]
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[[Category: fmn]]
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[[Category: Fmn]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 02:03:41 2008''
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Revision as of 23:03, 3 May 2008

Image:2e77.jpg

Template:STRUCTURE 2e77

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 Sun May 4 02:03:41 2008

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