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| | <StructureSection load='4js2' size='340' side='right'caption='[[4js2]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='4js2' size='340' side='right'caption='[[4js2]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4js2]] is a 1 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=4JS2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JS2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4js2]] is a 1 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=4JS2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JS2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4js1|4js1]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=C5P:CYTIDINE-5-MONOPHOSPHATE'>C5P</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4js2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4js2 OCA], [https://pdbe.org/4js2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4js2 RCSB], [https://www.ebi.ac.uk/pdbsum/4js2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4js2 ProSAT]</span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4js2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4js2 OCA], [http://pdbe.org/4js2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4js2 RCSB], [http://www.ebi.ac.uk/pdbsum/4js2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4js2 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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| | ==See Also== | | ==See Also== |
| - | *[[Sialyltransferase|Sialyltransferase]] | + | *[[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: Benz, J]] | + | [[Category: Benz J]] |
| - | [[Category: Engel, A M]] | + | [[Category: Engel AM]] |
| - | [[Category: Greif, M]] | + | [[Category: Greif M]] |
| - | [[Category: Kuhn, B]] | + | [[Category: Kuhn B]] |
| - | [[Category: Rudolph, M G]] | + | [[Category: Rudolph MG]] |
| - | [[Category: Sobek, H]] | + | [[Category: Sobek H]] |
| - | [[Category: Endoplasmatic reticulum]]
| + | |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Golgi]]
| + | |
| - | [[Category: Gt-a]]
| + | |
| - | [[Category: Rossmann]]
| + | |
| - | [[Category: Sialylation]]
| + | |
| - | [[Category: Sialyltransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
4js2 is a 1 chain structure with sequence from Homo sapiens. 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
SIAT1_HUMAN Transfers sialic acid from the donor of substrate CMP-sialic acid to galactose containing acceptor substrates.[1]
Publication Abstract from PubMed
Human beta-galactoside alpha-2,6-sialyltransferase I (ST6Gal-I) establishes the final glycosylation pattern of many glycoproteins by transferring a sialyl moiety to a terminal galactose. Complete sialylation of therapeutic immunoglobulins is essential for their anti-inflammatory activity and protein stability, but is difficult to achieve in vitro owing to the limited activity of ST6Gal-I towards some galactose acceptors. No structural information on ST6Gal-I that could help to improve the enzymatic properties of ST6Gal-I for biotechnological purposes is currently available. Here, the crystal structures of human ST6Gal-I in complex with the product cytidine 5'-monophosphate and in complex with cytidine and phosphate are described. These complexes allow the rationalization of the inhibitory activity of cytosine-based nucleotides. ST6Gal-I adopts a variant of the canonical glycosyltransferase A fold and differs from related sialyltransferases by several large insertions and deletions that determine its regiospecificity and substrate specificity. A large glycan from a symmetry mate localizes to the active site of ST6Gal-I in an orientation compatible with catalysis. The glycan binding mode can be generalized to any glycoprotein that is a substrate of ST6Gal-I. Comparison with a bacterial sialyltransferase in complex with a modified sialyl donor lends insight into the Michaelis complex. The results support an SN2 mechanism with inversion of configuration at the sialyl residue and suggest substrate-assisted catalysis with a charge-relay mechanism that bears a conceptual similarity to serine proteases.
The structure of human alpha-2,6-sialyltransferase reveals the binding mode of complex glycans.,Kuhn B, Benz J, Greif M, Engel AM, Sobek H, Rudolph MG Acta Crystallogr D Biol Crystallogr. 2013 Sep;69(Pt 9):1826-38. doi:, 10.1107/S0907444913015412. Epub 2013 Aug 17. PMID:23999306[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
- ↑ Kuhn B, Benz J, Greif M, Engel AM, Sobek H, Rudolph MG. The structure of human alpha-2,6-sialyltransferase reveals the binding mode of complex glycans. Acta Crystallogr D Biol Crystallogr. 2013 Sep;69(Pt 9):1826-38. doi:, 10.1107/S0907444913015412. Epub 2013 Aug 17. PMID:23999306 doi:http://dx.doi.org/10.1107/S0907444913015412
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