4ag7: Difference between revisions
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<StructureSection load='4ag7' size='340' side='right'caption='[[4ag7]], [[Resolution|resolution]] 1.55Å' scene=''> | <StructureSection load='4ag7' size='340' side='right'caption='[[4ag7]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ag7]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ag7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AG7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ag9|4ag9]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4ag9|4ag9]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glucosamine-phosphate_N-acetyltransferase Glucosamine-phosphate N-acetyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.4 2.3.1.4] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ag7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ag7 OCA], [https://pdbe.org/4ag7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ag7 RCSB], [https://www.ebi.ac.uk/pdbsum/4ag7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ag7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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[[Category: Caeel]] | [[Category: Caeel]] | ||
[[Category: Glucosamine-phosphate N-acetyltransferase]] | [[Category: Glucosamine-phosphate N-acetyltransferase]] | ||
[[Category: Large Structures]] | |||
[[Category: Aalten, D M.F van]] | [[Category: Aalten, D M.F van]] | ||
[[Category: Attrill, H]] | [[Category: Attrill, H]] | ||
Latest revision as of 08:33, 25 August 2022
C. elegans glucosamine-6-phosphate N-acetyltransferase (GNA1): coenzyme A adductC. elegans glucosamine-6-phosphate N-acetyltransferase (GNA1): coenzyme A adduct
Structural highlights
Publication Abstract from PubMedGlucosamine-6-phosphate N-acetyltransferase 1 (GNA1) produces GlcNAc-6-phosphate from GlcN-6-phosphate and acetyl coenzyme A. Early mercury-labelling experiments implicated a conserved cysteine in the reaction mechanism, whereas recent structural data appear to support a mechanism in which this cysteine plays no role. Here, two crystal structures of Caenorhabditis elegans GNA1 are reported, revealing an unusual covalent complex between this cysteine and the coenzyme A product. Mass-spectrometric and reduction studies showed that this inactive covalent complex can be reactivated through reduction, yet mutagenesis of the cysteine supports a previously reported bi-bi mechanism. The data unify the apparently contradictory earlier reports on the role of a cysteine in the GNA1 active site. Structural and biochemical characterization of a trapped coenzyme A adduct of Caenorhabditis elegans glucosamine-6-phosphate N-acetyltransferase 1.,Dorfmueller HC, Fang W, Rao FV, Blair DE, Attrill H, van Aalten DM Acta Crystallogr D Biol Crystallogr. 2012 Aug;68(Pt 8):1019-29. Epub 2012 Jul 17. PMID:22868768[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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