2e77

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[[Image:2e77.jpg|left|200px]]<br /><applet load="2e77" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2e77.jpg|left|200px]]
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caption="2e77, resolution 1.90&Aring;" />
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'''Crystal structure of L-lactate oxidase with pyruvate complex'''<br />
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{{Structure
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|PDB= 2e77 |SIZE=350|CAPTION= <scene name='initialview01'>2e77</scene>, resolution 1.90&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene> and <scene name='pdbligand=PYR:PYRUVIC ACID'>PYR</scene>
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|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]
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|GENE=
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}}
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'''Crystal structure of L-lactate oxidase with pyruvate complex'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2E77 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aerococcus_viridans Aerococcus viridans] with <scene name='pdbligand=FMN:'>FMN</scene> and <scene name='pdbligand=PYR:'>PYR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E77 OCA].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=17517371 17517371]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:06:48 2008''
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''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


PDB ID 2e77

Drag the structure with the mouse to rotate
, 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

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