This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3t90

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 10:01, 4 August 2016

Crystal structure of glucosamine-6-phosphate N-acetyltransferase from Arabidopsis thaliana

Structural highlights

3t90 is a 1 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	F14F8_150, GNA1, At5g15770, AT5G15770 (ARATH)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3t90"

@@ Line 1: / Line 1: @@
 ==Crystal structure of glucosamine-6-phosphate N-acetyltransferase from Arabidopsis thaliana==
 <StructureSection load='3t90' size='340' side='right' caption='[[3t90]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3t90]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. 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 [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>
 </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>
-<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 Arabidopsis thaliana])</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='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://www.rcsb.org/pdb/explore.do?structureId=3t90 RCSB], [http://www.ebi.ac.uk/pdbsum/3t90 PDBsum]</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=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>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/Q9LFU9_ARATH Q9LFU9_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:22932674</ref> <ref>PMID:22329777</ref>
+[[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3t90" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Arabidopsis thaliana]]
+[[Category: Arath]]
 [[Category: Grishkovskaya, I]]
 [[Category: Herter, T]]

3t90

From Proteopedia

Revision as of 10:01, 4 August 2016

Crystal structure of glucosamine-6-phosphate N-acetyltransferase from Arabidopsis thaliana

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox