|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of Aspergillus fumigatus N-acetylphosphoglucosamine mutase in complex with GlcNAc-6P and magnesium== | | ==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=''> | + | <StructureSection load='5oaw' size='340' side='right'caption='[[5oaw]], [[Resolution|resolution]] 2.34Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5oaw]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OAW FirstGlance]. <br> | + | <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='ligand'><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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALT_8497 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=293939 Aspergillus lentulus])</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> |
| - | <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=5oaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oaw OCA], [http://pdbe.org/5oaw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oaw RCSB], [http://www.ebi.ac.uk/pdbsum/5oaw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oaw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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] | + | [https://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 26: |
Line 24: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Aspergillus lentulus]] | | [[Category: Aspergillus lentulus]] |
| - | [[Category: Phosphoacetylglucosamine mutase]] | + | [[Category: Large Structures]] |
| - | [[Category: Hurtado-Guerrero, R]] | + | [[Category: Hurtado-Guerrero R]] |
| - | [[Category: Raimi, O G]] | + | [[Category: Raimi OG]] |
| - | [[Category: Aspergillus fumigatus]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Mutase]]
| + | |
| - | [[Category: N-acetylphosphoglucosamine]]
| + | |
| Structural highlights
Function
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]
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Raimi OG, Hurtado Guerrero R, van Aalten DM. Evidence for substrate assisted catalysis in N-acetylphosphoglucosamine mutase. Biochem J. 2018 Jul 2. pii: BCJ20180172. doi: 10.1042/BCJ20180172. PMID:29967067 doi:http://dx.doi.org/10.1042/BCJ20180172
|
