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==C. elegans glucosamine-6-phosphate N-acetyltransferase (GNA1): coenzyme A adduct== | |||
<StructureSection load='4ag7' size='340' side='right'caption='[[4ag7]], [[Resolution|resolution]] 1.55Å' scene=''> | |||
== Structural highlights == | |||
<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" 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"><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'>[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'>[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> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
== | </div> | ||
<div class="pdbe-citations 4ag7" style="background-color:#fffaf0;"></div> | |||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Caeel]] | |||
[[Category: Glucosamine-phosphate N-acetyltransferase]] | [[Category: Glucosamine-phosphate N-acetyltransferase]] | ||
[[Category: Aalten, D M.F | [[Category: Large Structures]] | ||
[[Category: Attrill, H | [[Category: Aalten, D M.F van]] | ||
[[Category: Blair, D E | [[Category: Attrill, H]] | ||
[[Category: Dorfmueller, H C | [[Category: Blair, D E]] | ||
[[Category: Fang, W | [[Category: Dorfmueller, H C]] | ||
[[Category: Rao, F V | [[Category: Fang, W]] | ||
[[Category: Shepherd, S M | [[Category: Rao, F V]] | ||
[[Category: Shepherd, S M]] | |||
[[Category: Transferase]] | [[Category: Transferase]] | ||
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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