4qnw: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
'''Unreleased structure'''
==Crystal structure of EasA, an old yellow enzyme from Aspergillus fumigatus==
<StructureSection load='4qnw' size='340' side='right' caption='[[4qnw]], [[Resolution|resolution]] 1.80&Aring;' 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.


The entry 4qnw is ON HOLD  until Paper Publication
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>


Authors: Lamb, A.L.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Crystal structure of EasA, an old yellow enzyme from Aspergillus fumigatus
== 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]]