5wro
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Drosophila enolase== | |
| + | <StructureSection load='5wro' size='340' side='right' caption='[[5wro]], [[Resolution|resolution]] 2.02Å' 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </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]] | ||
Revision as of 13:54, 27 April 2017
Crystal structure of Drosophila enolase
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