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| | <StructureSection load='6qvt' size='340' side='right'caption='[[6qvt]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='6qvt' size='340' side='right'caption='[[6qvt]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6qvt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QVT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6QVT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6qvt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QVT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QVT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NCC:CYTIDINE-5-MONOPHOSPHATE-5-N-ACETYLNEURAMINIC+ACID'>NCC</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 1.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ST6GAL1, SIAT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NCC:CYTIDINE-5-MONOPHOSPHATE-5-N-ACETYLNEURAMINIC+ACID'>NCC</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-galactoside_alpha-2,6-sialyltransferase Beta-galactoside alpha-2,6-sialyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.99.1 2.4.99.1] </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=6qvt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qvt OCA], [https://pdbe.org/6qvt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qvt RCSB], [https://www.ebi.ac.uk/pdbsum/6qvt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qvt ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6qvt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qvt OCA], [http://pdbe.org/6qvt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qvt RCSB], [http://www.ebi.ac.uk/pdbsum/6qvt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qvt ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SIAT1_HUMAN SIAT1_HUMAN]] Transfers sialic acid from the donor of substrate CMP-sialic acid to galactose containing acceptor substrates.<ref>PMID:21081508</ref> | + | [https://www.uniprot.org/uniprot/SIAT1_HUMAN SIAT1_HUMAN] Transfers sialic acid from the donor of substrate CMP-sialic acid to galactose containing acceptor substrates.<ref>PMID:21081508</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6qvt" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6qvt" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Sialyltransferase 3D structures|Sialyltransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Beta-galactoside alpha-2,6-sialyltransferase]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Glumoff, T]] | + | [[Category: Glumoff T]] |
| - | [[Category: Harrus, D]] | + | [[Category: Harrus D]] |
| - | [[Category: 6-sialyltransferase 1]]
| + | |
| - | [[Category: Beta-galactoside alpha-2]]
| + | |
| - | [[Category: Cmp-neu5ac]]
| + | |
| - | [[Category: Cmp-sia]]
| + | |
| - | [[Category: Cmp-sialic acid]]
| + | |
| - | [[Category: Cytidine-5'-monophospho-n-acetylneuraminic]]
| + | |
| - | [[Category: N-linked glycosylation]]
| + | |
| - | [[Category: Sialic acid]]
| + | |
| - | [[Category: Sialyltransferase]]
| + | |
| - | [[Category: St6gal1]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
SIAT1_HUMAN Transfers sialic acid from the donor of substrate CMP-sialic acid to galactose containing acceptor substrates.[1]
Publication Abstract from PubMed
Sialic acid residues found as terminal monosaccharides in various types of glycan chains in cell surface glycoproteins and glycolipids have been identified as important contributors of cell-cell interactions in normal vs. abnormal cellular behavior and are pivotal in diseases such as cancers. In vertebrates, sialic acids are attached to glycan chains by a conserved subset of sialyltransferases with different enzymatic and substrate specificities. ST6Gal I is a sialyltransferase using activated CMP-sialic acids as donor substrates to catalyze the formation of a alpha2,6-glycosidic bond between the sialic acid residue and the acceptor disaccharide LacNAc. Understanding sialyltransferases at the molecular and structural level shed light into their function. We present here two human ST6Gal I structures, which show for the first time the enzyme in the unliganded state and with the full donor substrate CMP-Neu5Ac bound. Comparison of these structures reveal flexibility of the catalytic loop, since in the unliganded structure Tyr354 adopts a conformation seen also as an alternate conformation in the substrate bound structure. CMP-Neu5Ac is bound with the side chain at C5 of the sugar residue directed outwards at the surface of the protein. Furthermore, the exact binding mode of the sialic acid moiety of the substrate directly involves sialylmotifs L, S and III and positions the sialylmotif VS in the immediate vicinity. We also present a model for the ternary complex of ST6Gal I with both the donor and the acceptor substrates.
Unliganded and CMP-Neu5Ac bound structures of human alpha-2,6-sialyltransferase ST6Gal I at high resolution.,Harrus D, Harduin-Lepers A, Glumoff T J Struct Biol. 2020 Sep 21;212(2):107628. doi: 10.1016/j.jsb.2020.107628. PMID:32971290[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wu ZL, Ethen CM, Prather B, Machacek M, Jiang W. Universal phosphatase-coupled glycosyltransferase assay. Glycobiology. 2011 Jun;21(6):727-33. doi: 10.1093/glycob/cwq187. Epub 2010 Nov, 15. PMID:21081508 doi:10.1093/glycob/cwq187
- ↑ Harrus D, Harduin-Lepers A, Glumoff T. Unliganded and CMP-Neu5Ac bound structures of human alpha-2,6-sialyltransferase ST6Gal I at high resolution. J Struct Biol. 2020 Sep 21;212(2):107628. doi: 10.1016/j.jsb.2020.107628. PMID:32971290 doi:http://dx.doi.org/10.1016/j.jsb.2020.107628
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