4ag9: Difference between revisions

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-[[Image:4ag9.png|left|200px]]
+==C. elegans glucosamine-6-phosphate N-acetyltransferase (GNA1): ternary complex with coenzyme A and GlcNAc==
+<StructureSection load='4ag9' size='340' side='right' caption='[[4ag9]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4ag9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AG9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AG9 FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=16G:N-ACETYL-D-GLUCOSAMINE-6-PHOSPHATE'>16G</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene><br>
+<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ag7|4ag7]]</td></tr>
+<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ag9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ag9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ag9 RCSB], [http://www.ebi.ac.uk/pdbsum/4ag9 PDBsum]</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.
-{{STRUCTURE_4ag9|  PDB=4ag9  |  SCENE=  }}
+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>
-===C. elegans glucosamine-6-phosphate N-acetyltransferase (GNA1): ternary complex with coenzyme A and GlcNAc===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_22868768}}
+== References ==
+<references/>
-==About this Structure==
+__TOC__
-[[4ag9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AG9 OCA].
+</StructureSection>
-==Reference==
-<ref group="xtra">PMID:022868768</ref><references group="xtra"/>
 [[Category: Caenorhabditis elegans]]
 [[Category: Glucosamine-phosphate N-acetyltransferase]]