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| <StructureSection load='3otk' size='340' side='right'caption='[[3otk]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='3otk' size='340' side='right'caption='[[3otk]], [[Resolution|resolution]] 2.30Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3otk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OTK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OTK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3otk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OTK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OTK FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HTO:HEPTANE-1,2,3-TRIOL'>HTO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</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]] 2.3Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Gcnt1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=HTO:HEPTANE-1,2,3-TRIOL'>HTO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-1,3-galactosyl-O-glycosyl-glycoprotein_beta-1,6-N-_acetylglucosaminyltransferase Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N- acetylglucosaminyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.102 2.4.1.102] </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=3otk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3otk OCA], [https://pdbe.org/3otk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3otk RCSB], [https://www.ebi.ac.uk/pdbsum/3otk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3otk 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=3otk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3otk OCA], [https://pdbe.org/3otk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3otk RCSB], [https://www.ebi.ac.uk/pdbsum/3otk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3otk ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[https://www.uniprot.org/uniprot/GCNT1_MOUSE GCNT1_MOUSE]] Forms critical branches in O-glycans.<ref>PMID:7983056</ref>
| + | [https://www.uniprot.org/uniprot/GCNT1_MOUSE GCNT1_MOUSE] Forms critical branches in O-glycans.<ref>PMID:7983056</ref> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N- acetylglucosaminyltransferase]] | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
- | [[Category: Pak, J E]] | + | [[Category: Pak JE]] |
- | [[Category: Rini, J M]] | + | [[Category: Rini JM]] |
- | [[Category: Glycosyltransferase]]
| + | |
- | [[Category: Golgi]]
| + | |
- | [[Category: Transferase]]
| + | |
| Structural highlights
3otk is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| Method: | X-ray diffraction, Resolution 2.3Å |
Ligands: | , , , , |
Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
GCNT1_MOUSE Forms critical branches in O-glycans.[1]
Publication Abstract from PubMed
Leukocyte-type core 2 beta1,6-N-acetylglucosaminyltransferase (C2GnT-L) is an inverting, metal-ion-independent glycosyltransferase that catalyzes the formation of mucin-type core 2 O-glycans. C2GnT-L belongs to the GT-A fold, yet it lacks the metal ion binding DXD motif characteristic of other nucleoside disphosphate GT-A fold glycosyltransferases. To shed light on the basis for its metal ion independence, we have solved the X-ray crystal structure (2.3 A resolution) of a mutant form of C2GnT-L (C217S) in complex with the nucleotide sugar product UDP and, using site-directed mutagenesis, examined the roles of R378 and K401 in both substrate binding and catalysis. The structure shows that C2GnT-L exists in an "open" conformation and a "closed" conformation and that, in the latter, R378 and K401 interact with the beta-phosphate moiety of the bound UDP. The two conformations are likely to be important in catalysis, but the conformational changes that lead to their interconversion do not resemble the nucleotide-sugar-mediated loop ordering observed in other GT-A glycosyltransferases. R378 and K401 were found to be important in substrate binding and/or catalysis, an observation consistent with the suggestion that they serve the same role played by metal ion in all of the other GT-A glycosyltransferases studied to date. Notably, R378 and K401 appear to function in a manner similar to that of the arginine and lysine residues contained in the RX(4-5)K motif found in the retaining GT-B glycosyltransferases.
Structural and mechanistic characterization of leukocyte-type core 2 beta1,6-N-acetylglucosaminyltransferase: a metal-ion-independent GT-A glycosyltransferase.,Pak JE, Satkunarajah M, Seetharaman J, Rini JM J Mol Biol. 2011 Dec 16;414(5):798-811. Epub 2011 Oct 26. PMID:22056345[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sekine M, Hashimoto Y, Suzuki M, Inagaki F, Takio K, Suzuki A. Purification and characterization of UDP-GlcNAc:IV3 beta Gal-Gb4Cer beta-1,6-GlcNAc transferase from mouse kidney. J Biol Chem. 1994 Dec 9;269(49):31143-8. PMID:7983056
- ↑ Pak JE, Satkunarajah M, Seetharaman J, Rini JM. Structural and mechanistic characterization of leukocyte-type core 2 beta1,6-N-acetylglucosaminyltransferase: a metal-ion-independent GT-A glycosyltransferase. J Mol Biol. 2011 Dec 16;414(5):798-811. Epub 2011 Oct 26. PMID:22056345 doi:10.1016/j.jmb.2011.10.039
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