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
Current revision (13:21, 14 March 2024) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
 +
==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]] 1.50&Aring;' scene=''>
+
<StructureSection load='3t90' size='340' side='right'caption='[[3t90]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== 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 [https://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 [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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</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='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='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'>[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/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>
+
[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;">
+
-
== 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<ref>PMID:22329777</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
== References ==
== References ==
<references/>
<references/>
Line 22: Line 15:
</StructureSection>
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
-
[[Category: Grishkovskaya, I]]
+
[[Category: Large Structures]]
-
[[Category: Herter, T]]
+
[[Category: Grishkovskaya I]]
-
[[Category: Riegler, H]]
+
[[Category: Herter T]]
-
[[Category: Usadel, B]]
+
[[Category: Riegler H]]
-
[[Category: Acetyltransferase]]
+
[[Category: Usadel B]]
-
[[Category: Alpha/beta protein]]
+
-
[[Category: Glcnac biosynthesis]]
+
-
[[Category: Gnat fold]]
+
-
[[Category: Transferase]]
+

Current revision

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

PDB ID 3t90

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

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