View source for 4ag7


==C. elegans glucosamine-6-phosphate N-acetyltransferase (GNA1): coenzyme A adduct==
<StructureSection load='4ag7' size='340' side='right' caption='[[4ag7]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ag7]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ag9|4ag9]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucosamine-phosphate_N-acetyltransferase Glucosamine-phosphate N-acetyltransferase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ag7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ag7 OCA], [http://pdbe.org/4ag7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ag7 RCSB], [http://www.ebi.ac.uk/pdbsum/4ag7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ag7 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glucosamine-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<ref>PMID:22868768</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ag7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Caeel]]
[[Category: Glucosamine-phosphate N-acetyltransferase]]
[[Category: Aalten, D M.F Van]]
[[Category: Attrill, H]]
[[Category: Blair, D E]]
[[Category: Dorfmueller, H C]]
[[Category: Fang, W]]
[[Category: Rao, F V]]
[[Category: Shepherd, S M]]
[[Category: Transferase]]