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| | ==Crystal structure of glucosamine-6-phosphate N-acetyltransferase from Arabidopsis thaliana== | | ==Crystal structure of glucosamine-6-phosphate N-acetyltransferase from Arabidopsis thaliana== |
| - | <StructureSection load='3t90' size='340' side='right' caption='[[3t90]], [[Resolution|resolution]] 1.50Å' scene=''> | + | <StructureSection load='3t90' size='340' side='right'caption='[[3t90]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3t90]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T90 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T90 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3t90]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T90 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T90 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">F14F8_150, GNA1, At5g15770, AT5G15770 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">F14F8_150, GNA1, At5g15770, AT5G15770 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=3t90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t90 OCA], [http://pdbe.org/3t90 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3t90 RCSB], [http://www.ebi.ac.uk/pdbsum/3t90 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3t90 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=3t90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t90 OCA], [https://pdbe.org/3t90 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t90 RCSB], [https://www.ebi.ac.uk/pdbsum/3t90 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t90 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GNA1_ARATH GNA1_ARATH]] Acetyltransferase involved in UDP-N-acetylglucosamine (UDP-GlcNAc) biosynthesis. UDP-GlcNAc is an essential metabolite that serves as an initial sugar donor for N-glycan synthesis and thus plays an important role in protein and lipid glycosylation.<ref>PMID:22329777</ref> <ref>PMID:22932674</ref> | + | [[https://www.uniprot.org/uniprot/GNA1_ARATH GNA1_ARATH]] Acetyltransferase involved in UDP-N-acetylglucosamine (UDP-GlcNAc) biosynthesis. UDP-GlcNAc is an essential metabolite that serves as an initial sugar donor for N-glycan synthesis and thus plays an important role in protein and lipid glycosylation.<ref>PMID:22329777</ref> <ref>PMID:22932674</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Arath]] | | [[Category: Arath]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Grishkovskaya, I]] | | [[Category: Grishkovskaya, I]] |
| | [[Category: Herter, T]] | | [[Category: Herter, T]] |
| Structural highlights
Function
[GNA1_ARATH] Acetyltransferase involved in UDP-N-acetylglucosamine (UDP-GlcNAc) biosynthesis. UDP-GlcNAc is an essential metabolite that serves as an initial sugar donor for N-glycan synthesis and thus plays an important role in protein and lipid glycosylation.[1] [2]
Publication Abstract from PubMed
GlcNAc (N-acetylglucosamine) is an essential part of the glycan chain in N-linked glycoproteins. It is a building block for polysaccharides such as chitin, and several glucosaminoglycans and proteins can be O-GlcNAcylated. The deacetylated form, glucosamine, is an integral part of GPI (glycosylphosphatidylinositol) anchors. Both are incorporated into polymers by glycosyltransferases that utilize UDP-GlcNAc. This UDP-sugar is synthesized in a short pathway comprising four steps starting from fructose 6-phosphate. GNA (glucosamine-6-phosphate N-acetyltransferase) catalyses the second of these four reactions in the de novo synthesis in eukaryotes. A phylogenetic analysis revealed that only one GNA isoform can be found in most of the species investigated and that the most likely Arabidopsis candidate is encoded by the gene At5g15770 (AtGNA). qPCR (quantitative PCR) revealed the ubiquitous expression of AtGNA in all organs of Arabidopsis plants. Heterologous expression of AtGNA showed that it is highly active between pH 7 and 8 and at temperatures of 30-40 degrees C. It showed Km values of 231 muM for glucosamine 6-phosphate and 33 muM for acetyl-CoA respectively and a catalytic efficiency comparable with that of other GNAs characterized. The solved crystal structure of AtGNA at a resolution of 1.5 A (1 A=0.1 nm) revealed a very high structural similarity to crystallized GNA proteins from Homo sapiens and Saccharomyces cerevisiae despite less well conserved protein sequence identity.
Crystal structure and functional characterization of a glucosamine-6-phosphate N-acetyltransferase from Arabidopsis thaliana.,Riegler H, Herter T, Grishkovskaya I, Lude A, Ryngajllo M, Bolger ME, Essigmann B, Usadel B Biochem J. 2012 Apr 15;443(2):427-37. PMID:22329777[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Riegler H, Herter T, Grishkovskaya I, Lude A, Ryngajllo M, Bolger ME, Essigmann B, Usadel B. Crystal structure and functional characterization of a glucosamine-6-phosphate N-acetyltransferase from Arabidopsis thaliana. Biochem J. 2012 Apr 15;443(2):427-37. PMID:22329777 doi:10.1042/BJ20112071
- ↑ Nozaki M, Sugiyama M, Duan J, Uematsu H, Genda T, Sato Y. A missense mutation in the glucosamine-6-phosphate N-acetyltransferase-encoding gene causes temperature-dependent growth defects and ectopic lignin deposition in Arabidopsis. Plant Cell. 2012 Aug;24(8):3366-79. Epub 2012 Aug 28. PMID:22932674 doi:http://dx.doi.org/10.1105/tpc.112.102806
- ↑ Riegler H, Herter T, Grishkovskaya I, Lude A, Ryngajllo M, Bolger ME, Essigmann B, Usadel B. Crystal structure and functional characterization of a glucosamine-6-phosphate N-acetyltransferase from Arabidopsis thaliana. Biochem J. 2012 Apr 15;443(2):427-37. PMID:22329777 doi:10.1042/BJ20112071
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