5wro: Difference between revisions

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'''Unreleased structure'''


The entry 5wro is ON HOLD  until Paper Publication
==Crystal structure of Drosophila enolase==
<StructureSection load='5wro' size='340' side='right' caption='[[5wro]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5wro]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WRO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WRO FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] </span></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=5wro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wro OCA], [http://pdbe.org/5wro PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wro RCSB], [http://www.ebi.ac.uk/pdbsum/5wro PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wro ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Enolase is an important enzyme in glycolysis and various biological processes. Its dysfunction is closely associated with diseases. Here, the enolase from Drosophila melanogaster (DmENO) was purified and crystallized. A crystal of DmENO diffracted to 2.0 A resolution and belonged to space group R32. The structure was solved by molecular replacement. Like most enolases, DmENO forms a homodimer with conserved residues in the dimer interface. DmENO possesses an open conformation in this structure and contains conserved elements for catalytic activity. This work provides a structural basis for further functional and evolutionary studies of enolase.


Authors:  
Crystal structure of enolase from Drosophila melanogaster.,Sun C, Xu B, Liu X, Zhang Z, Su Z Acta Crystallogr F Struct Biol Commun. 2017 Apr 1;73(Pt 4):228-234. doi:, 10.1107/S2053230X17004022. Epub 2017 Mar 22. PMID:28368282<ref>PMID:28368282</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5wro" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Phosphopyruvate hydratase]]
[[Category: Shi, Z]]
[[Category: Zhang, Z]]
[[Category: Enolase]]
[[Category: Hydrolyase]]
[[Category: Lyase]]
[[Category: Metabolism]]
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