5dqp
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==EDTA monooxygenase (EmoA) from Chelativorans sp. BNC1== | |
| + | <StructureSection load='5dqp' size='340' side='right' caption='[[5dqp]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5dqp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DQP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DQP FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PE4:2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>PE4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5dqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dqp OCA], [http://pdbe.org/5dqp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dqp RCSB], [http://www.ebi.ac.uk/pdbsum/5dqp PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Ethylenediaminetetraacetate (EDTA) is currently the most abundant organic pollutant due to its recalcitrance and extensive use. Only a few bacteria can degrade it, using EDTA monooxygenase (EmoA) to initiate the degradation. EmoA is an FMNH2 -dependent monooxygenase that requires an NADH:FMN oxidoreductase (EmoB) to provide FMNH2 as a cosubstrate. Although EmoA has been identified from Chelativorans (ex. Mesorhizobium) sp. BNC1, its catalytic mechanism is unknown. Crystal structures of EmoA revealed a domain-like insertion into a TIM-barrel, which might serve as a flexible lid for the active site. Docking of MgEDTA2- into EmoA identified an intricate hydrogen bond network connected to Tyr71 , which should potentially lower its pKa. Tyr71 , along with nearby Glu70 and a peroxy flavin, facilitates a keto-enol transition of the leaving acetyl group of EDTA. Further, for the first time, the physical interaction between EmoA and EmoB was observed by ITC, molecular docking and enzyme kinetic assay, which enhanced both EmoA and EmoB activities probably through coupled channeling of FMNH2 . This article is protected by copyright. All rights reserved. | ||
| - | + | Structural and Biochemical Characterization of EDTA Monooxygenase and its Physical Interaction with a Partner Flavin Reductase.,Jun SY, Lewis KM, Youn B, Xun L, Kang C Mol Microbiol. 2016 Feb 29. doi: 10.1111/mmi.13363. PMID:26928990<ref>PMID:26928990</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5dqp" style="background-color:#fffaf0;"></div> | |
| - | [[Category: Jun, S | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Jun, S Y]] | ||
[[Category: Kang, C]] | [[Category: Kang, C]] | ||
| - | [[Category: Lewis, K | + | [[Category: Lewis, K M]] |
| + | [[Category: Xun, L]] | ||
[[Category: Youn, B]] | [[Category: Youn, B]] | ||
| + | [[Category: Bioremediation]] | ||
| + | [[Category: Edta degradation]] | ||
| + | [[Category: Monooxygenase]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 03:48, 11 May 2016
EDTA monooxygenase (EmoA) from Chelativorans sp. BNC1
| |||||||||||
