4ag9: Difference between revisions
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<StructureSection load='4ag9' size='340' side='right'caption='[[4ag9]], [[Resolution|resolution]] 1.76Å' scene=''> | <StructureSection load='4ag9' size='340' side='right'caption='[[4ag9]], [[Resolution|resolution]] 1.76Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ag9]] is a 2 chain structure. 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 [https://proteopedia.org/fgij/fg.htm?mol=4AG9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4ag9]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=4AG9 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></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=4ag9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ag9 OCA], [https://pdbe.org/4ag9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ag9 RCSB], [https://www.ebi.ac.uk/pdbsum/4ag9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ag9 ProSAT]</span></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=4ag9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ag9 OCA], [https://pdbe.org/4ag9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ag9 RCSB], [https://www.ebi.ac.uk/pdbsum/4ag9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ag9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/GNA1_CAEEL GNA1_CAEEL] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 22: | Line 23: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Caenorhabditis elegans]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Attrill H]] | |||
[[Category: Attrill | [[Category: Blair DE]] | ||
[[Category: Blair | [[Category: Dorfmueller HC]] | ||
[[Category: Dorfmueller | [[Category: Fang W]] | ||
[[Category: Fang | [[Category: Rao FV]] | ||
[[Category: Rao | [[Category: Shepherd SM]] | ||
[[Category: Shepherd | [[Category: Van Aalten DMF]] | ||
[[Category: | |||
Latest revision as of 14:26, 20 December 2023
C. elegans glucosamine-6-phosphate N-acetyltransferase (GNA1): ternary complex with coenzyme A and GlcNAcC. elegans glucosamine-6-phosphate N-acetyltransferase (GNA1): ternary complex with coenzyme A and GlcNAc
Structural highlights
FunctionPublication 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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