View source for 4uir


==Structure of oleate hydratase from Elizabethkingia meningoseptica==
<StructureSection load='4uir' size='340' side='right'caption='[[4uir]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4uir]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Elizabethkingia_meningoseptica Elizabethkingia meningoseptica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UIR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4uir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uir OCA], [https://pdbe.org/4uir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uir RCSB], [https://www.ebi.ac.uk/pdbsum/4uir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uir ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OLHYD_ELIME OLHYD_ELIME] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Hydratases provide access to secondary and tertiary alcohols by regio- and/or stereospecifically adding water to carbon-carbon double bonds. Thereby, hydroxyl groups are introduced without the need for costly co-factor recycling, which renders this approach highly interesting on an industrial scale. Here, we present the first crystal structure of a recombinant oleate hydratase originating from Elizabethkingia meningoseptica in the presence of the flavin cofactor (FAD). A structure-based mutagenesis study targeting active site residues identified E122 and Y241 as crucial for the activation of a water molecule and protonation of the double bond, respectively. Moreover, we also observed that two-electron reduction of FAD results in a 7-fold increase of substrate hydration rate. We propose the first reaction mechanism for this enzyme class that rationalizes the requirement of flavin cofactor and the involvement of conserved amino acid residues in this regio- and stereoselective hydration.

Structure-based mechanism of oleate hydratase from Elizabethkingia meningoseptica.,Engleder M, Pavkov-Keller T, Emmerstorfer A, Hromic A, Schrempf S, Steinkellner G, Wriessnegger T, Leitner E, Strohmeier GA, Kaluzna I, Mink D, Schurmann M, Wallner S, Macheroux P, Gruber K, Pichler H Chembiochem. 2015 Jun 15. doi: 10.1002/cbic.201500269. PMID:26077980<ref>PMID:26077980</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4uir" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Elizabethkingia meningoseptica]]
[[Category: Large Structures]]
[[Category: Emmerstorfer A]]
[[Category: Engleder M]]
[[Category: Gruber K]]
[[Category: Hromic A]]
[[Category: Kaluzna I]]
[[Category: Leitner E]]
[[Category: Macheroux P]]
[[Category: Mink D]]
[[Category: Pavkov-Keller T]]
[[Category: Pichler H]]
[[Category: Schrempf S]]
[[Category: Schuermann M]]
[[Category: Steinkellner G]]
[[Category: Strohmeier GA]]
[[Category: Wallner S]]
[[Category: Wriessnegger T]]