4qnw
From Proteopedia
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| - | ''' | + | ==Crystal structure of EasA, an old yellow enzyme from Aspergillus fumigatus== |
| + | <StructureSection load='4qnw' size='340' side='right' caption='[[4qnw]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4qnw]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QNW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QNW FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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/Chanoclavine-I_aldehyde_reductase Chanoclavine-I aldehyde reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.100 1.3.1.100] </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=4qnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qnw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qnw RCSB], [http://www.ebi.ac.uk/pdbsum/4qnw PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The Aspergillus fumigatus old yellow enzyme (OYE) EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine aldehyde and works in conjunction with festuclavine synthase at the branchpoint for ergot alkaloid pathways. The crystal structure of the FMN-loaded EasA was determined to 1.8 A resolution. The active-site amino acids of OYE are conserved, supporting a similar mechanism for reduction of the alpha/beta-unsaturated aldehyde. The C-terminal tail of one monomer packs into the active site of a monomer in the next asymmetric unit, which is most likely to be a crystallization artifact and not a mechanism of self-regulation. | ||
| - | + | Structure of an Aspergillus fumigatus old yellow enzyme (EasA) involved in ergot alkaloid biosynthesis.,Chilton AS, Ellis AL, Lamb AL Acta Crystallogr F Struct Biol Commun. 2014 Oct 1;70(Pt 10):1328-32. doi:, 10.1107/S2053230X14018962. Epub 2014 Sep 25. PMID:25286934<ref>PMID:25286934</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Chanoclavine-I aldehyde reductase]] | ||
| + | [[Category: Lamb, A L.]] | ||
| + | [[Category: Alpha/beta barrel]] | ||
| + | [[Category: Ergot alkaloid]] | ||
| + | [[Category: Old yellow enzyme]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Reductase]] | ||
Revision as of 11:45, 22 October 2014
Crystal structure of EasA, an old yellow enzyme from Aspergillus fumigatus
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