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5o9x
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Aspergillus fumigatus N-acetylphosphoglucosamine mutate S69A in complex with glucose1,6bisphosphate== | |
| + | <StructureSection load='5o9x' size='340' side='right' caption='[[5o9x]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5o9x]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O9X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5O9X FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=G16:ALPHA-D-GLUCOSE+1,6-BISPHOSPHATE'>G16</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoacetylglucosamine_mutase Phosphoacetylglucosamine mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.3 5.4.2.3] </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=5o9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o9x OCA], [http://pdbe.org/5o9x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o9x RCSB], [http://www.ebi.ac.uk/pdbsum/5o9x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o9x ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/A0A0S7E9S6_9EURO A0A0S7E9S6_9EURO]] Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, which is a biosynthetic precursor of chitin and also supplies the amino sugars for N-linked oligosaccharides of glycoproteins.[PIRNR:PIRNR016408] | ||
| + | <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> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 5o9x" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Phosphoacetylglucosamine mutase]] | ||
[[Category: Hurtado-Guerrero, R]] | [[Category: Hurtado-Guerrero, R]] | ||
| + | [[Category: Raimi, O G]] | ||
| + | [[Category: Aspergillus fumigatus]] | ||
| + | [[Category: Mutase]] | ||
| + | [[Category: N-acetylphosphoglucosamine]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 05:34, 11 July 2018
Crystal structure of Aspergillus fumigatus N-acetylphosphoglucosamine mutate S69A in complex with glucose1,6bisphosphate
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