View source for 6lvp


==Enoyl-CoA hydratase (HyECH) from Hymenobacter sp. PAMC 26628==
<StructureSection load='6lvp' size='340' side='right'caption='[[6lvp]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6lvp]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Hymenobacter_sp._PAMC_26628 Hymenobacter sp. PAMC 26628]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LVP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LVP 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]] 2.69&#8491;</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=6lvp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lvp OCA], [https://pdbe.org/6lvp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lvp RCSB], [https://www.ebi.ac.uk/pdbsum/6lvp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lvp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A126PEF4_9BACT A0A126PEF4_9BACT] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Crystal structures of enoyl-coenzyme A (CoA) isomerase from Bosea sp. PAMC 26642 (BoECI) and enoyl-CoA hydratase from Hymenobacter sp. PAMC 26628 (HyECH) were determined at 2.35 and 2.70 A resolution, respectively. BoECI and HyECH are members of the crotonase superfamily and are enzymes known to be involved in fatty acid degradation. Structurally, these enzymes are highly similar except for the orientation of their C-terminal helix domain. Analytical ultracentrifugation was performed to determine the oligomerization states of BoECI and HyECH revealing they exist as trimers in solution. However, their putative ligand-binding sites and active site residue compositions are dissimilar. Comparative sequence and structural analysis revealed that the active site of BoECI had one glutamate residue (Glu135), this site is occupied by an aspartate in some ECIs, and the active sites of HyECH had two highly conserved glutamate residues (Glu118 and Glu138). Moreover, HyECH possesses a salt bridge interaction between Glu98 and Arg152 near the active site. This interaction may allow the catalytic Glu118 residue to have a specific conformation for the ECH enzyme reaction. This salt bridge interaction is highly conserved in known bacterial ECH structures and ECI enzymes do not have this type of interaction. Collectively, our comparative sequential and structural studies have provided useful information to distinguish and classify two similar bacterial crotonase superfamily enzymes.

Structural and sequence comparisons of bacterial enoyl-CoA isomerase and enoyl-CoA hydratase.,Hwang J, Jeong CS, Lee CW, Shin SC, Kim HW, Lee SG, Youn UJ, Lee CS, Oh TJ, Kim HJ, Park H, Park HH, Lee JH J Microbiol. 2020 Jul;58(7):606-613. doi: 10.1007/s12275-020-0089-1. Epub 2020, Apr 22. PMID:32323197<ref>PMID:32323197</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6lvp" style="background-color:#fffaf0;"></div>

==See Also==
*[[Enoyl-CoA hydratase 3D structures|Enoyl-CoA hydratase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Hymenobacter sp. PAMC 26628]]
[[Category: Large Structures]]
[[Category: Hwang JS]]
[[Category: Jung C]]
[[Category: Lee CW]]
[[Category: Lee JH]]