5oaw
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Aspergillus fumigatus N-acetylphosphoglucosamine mutase in complex with GlcNAc-6P and magnesium== | |
| + | <StructureSection load='5oaw' size='340' side='right'caption='[[5oaw]], [[Resolution|resolution]] 2.34Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5oaw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_lentulus Aspergillus lentulus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OAW FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.34Å</td></tr> | ||
| + | <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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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=5oaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oaw OCA], [https://pdbe.org/5oaw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oaw RCSB], [https://www.ebi.ac.uk/pdbsum/5oaw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oaw ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | N -acetylphosphoglucosamine mutase (AGM1) is a key component of the hexosamine biosynthetic pathway that produces UDP-GlcNAc, an essential precursor for a wide range of glycans in eukaryotes. AGM belongs to the a-D-phosphohexomutase metalloenzyme superfamily and catalyses the interconversion of N -acetylglucosamine-6-phosphate (GlcNAc-6P) to N -acetylglucosamine-1-phosphate (GlcNAc-1P) through N -acetylglucosamine-1,6-bisphosphate (GlcNAc-1,6-bisP) as the catalytic intermediate. Although there is an understanding of the phosphoserine-dependent catalytic mechanism at enzymatic and structural level, the identity of the requisite catalytic base in AGM1/phosphoglucomutases is as yet unknown. Here we present crystal structures of a Michaelis complex of AGM1 with GlcNAc-6P and Mg(2+), and a complex of the inactive Ser69Ala mutant together with glucose-1,6-bisphosphate (Glc-1,6-bisP) that represent key snapshots along the reaction coordinate. Together with mutagenesis, these structures reveal that the phosphate group of the hexose-1,6-bisP intermediate may act as the catalytic base. | ||
| - | + | Evidence for substrate assisted catalysis in N-acetylphosphoglucosamine mutase.,Raimi OG, Hurtado Guerrero R, van Aalten DM Biochem J. 2018 Jul 2. pii: BCJ20180172. doi: 10.1042/BCJ20180172. PMID:29967067<ref>PMID:29967067</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5oaw" style="background-color:#fffaf0;"></div> |
| - | [[Category: Hurtado-Guerrero | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Aspergillus lentulus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Hurtado-Guerrero R]] | ||
| + | [[Category: Raimi OG]] | ||
Current revision
Crystal structure of Aspergillus fumigatus N-acetylphosphoglucosamine mutase in complex with GlcNAc-6P and magnesium
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