2e77: Difference between revisions
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<StructureSection load='2e77' size='340' side='right'caption='[[2e77]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='2e77' size='340' side='right'caption='[[2e77]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2e77]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2e77]] is a 4 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E77 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2du2|2du2]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2du2|2du2]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lactate_2-monooxygenase Lactate 2-monooxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.12.4 1.13.12.4] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2e77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e77 OCA], [https://pdbe.org/2e77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e77 RCSB], [https://www.ebi.ac.uk/pdbsum/2e77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e77 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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</div> | </div> | ||
<div class="pdbe-citations 2e77" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2e77" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 20:21, 15 December 2021
Crystal structure of L-lactate oxidase with pyruvate complexCrystal structure of L-lactate oxidase with pyruvate complex
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedL-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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