7cys: Difference between revisions

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'''Unreleased structure'''


The entry 7cys is ON HOLD
==Crystal structure of barley agmatine coumaroyltransferase (HvACT), an N-acyltransferase in BAHD superfamily==
<StructureSection load='7cys' size='340' side='right'caption='[[7cys]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CYS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CYS 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]] 1.81&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene></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=7cys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cys OCA], [https://pdbe.org/7cys PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cys RCSB], [https://www.ebi.ac.uk/pdbsum/7cys PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cys ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The enzymes of the BAHD superfamily, a large group of acyl-CoA-dependent acyltransferases in plants, are involved in the biosynthesis of diverse secondary metabolites. While the structures of several O-acyltransferases from the BAHD superfamily, such as hydroxycinnamoyl-CoA shikimate hydroxycinnamoyl transferase, have been elucidated, no structural information on N-acyltransferases is available. Hordeum vulgare agmatine coumaroyltransferase (HvACT) is an N-acyltransferase from the BAHD superfamily and is one of the most important enzymes in the secondary metabolism of barley. Here, an apo-form structure of HvACT is reported as the first structure of an N-acyltransferase from the BAHD superfamily. HvACT crystals diffracted to 1.8 A resolution and belonged to the monoclinic space group P21, with unit-cell parameters a = 57.6, b = 59.5, c = 73.6 A, alpha = 90, beta = 91.3 , gamma = 90 degrees . Like other known BAHD superfamily structures, HvACT contains two domains that adopt a two-layer alphabeta-sandwich architecture and a solvent-exposed channel that penetrates the enzyme core.


Authors: Yamane, M., Takenoya, M., Sue, M., Yajima, S.
Crystal structure of barley agmatine coumaroyltransferase, an N-acyltransferase from the BAHD superfamily.,Yamane M, Takenoya M, Yajima S, Sue M Acta Crystallogr F Struct Biol Commun. 2020 Dec 1;76(Pt 12):590-596. doi:, 10.1107/S2053230X20014880. Epub 2020 Nov 25. PMID:33263570<ref>PMID:33263570</ref>


Description: Crystal structure of barley agmatine coumaroyltransferase (HvACT), an N-acyltransferase in BAHD superfamily
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Sue, M]]
<div class="pdbe-citations 7cys" style="background-color:#fffaf0;"></div>
[[Category: Yamane, M]]
== References ==
[[Category: Takenoya, M]]
<references/>
[[Category: Yajima, S]]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sue M]]
[[Category: Takenoya M]]
[[Category: Yajima S]]
[[Category: Yamane M]]
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