This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2e77
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2e77.jpg|left|200px]] | + | [[Image:2e77.jpg|left|200px]] |
| - | + | ||
| - | '''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== | ||
| Line 7: | Line 16: | ||
==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]] | ||
| Line 21: | Line 30: | ||
[[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
