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| | <StructureSection load='2x63' size='340' side='right'caption='[[2x63]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='2x63' size='340' side='right'caption='[[2x63]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2x63]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"campylobacter_fetus_subsp._jejuni"_smibert_1974 "campylobacter fetus subsp. jejuni" smibert 1974]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X63 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2X63 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2x63]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X63 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X63 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ro8|1ro8]], [[2x62|2x62]], [[1ro7|1ro7]], [[2x61|2x61]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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=2x63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x63 OCA], [http://pdbe.org/2x63 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x63 RCSB], [http://www.ebi.ac.uk/pdbsum/2x63 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x63 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=2x63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x63 OCA], [https://pdbe.org/2x63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x63 RCSB], [https://www.ebi.ac.uk/pdbsum/2x63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x63 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9LAK3_CAMJU Q9LAK3_CAMJU] |
| | <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: Campylobacter fetus subsp. jejuni smibert 1974]] | + | [[Category: Campylobacter jejuni]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lairson, L L]] | + | [[Category: Lairson LL]] |
| - | [[Category: Lee, H J]] | + | [[Category: Lee HJ]] |
| - | [[Category: Rich, J R]] | + | [[Category: Rich JR]] |
| - | [[Category: Strynadka, N C.J]] | + | [[Category: Strynadka NCJ]] |
| - | [[Category: Wakarchuk, W W]] | + | [[Category: Wakarchuk WW]] |
| - | [[Category: Withers, S G]] | + | [[Category: Withers SG]] |
| - | [[Category: Glycosyltransferase]]
| + | |
| - | [[Category: Gta]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q9LAK3_CAMJU
Publication Abstract from PubMed
Sialic acids play important roles in various biological processes and typically terminate the oligosaccharide chains on the cell surfaces of a wide range of organisms including mammals and bacteria. Their attachment is catalyzed by a set of sialyltransferases with defined specificities both for their acceptor sugars and the position of attachment. However, little is known of how this specificity is encoded. The structure of the bifunctional sialyltransferase Cst-II of the human pathogen Campylobacter jejuni in complex with CMP and the terminal trisaccharide of its natural acceptor (Neu5Ac-alpha-2,3-Gal-beta-1,3-GalNAc) has been solved at 1.95 A resolution and its kinetic mechanism shown to be iso-ordered Bi Bi, consistent with its dual acceptor substrate specificity. The trisaccharide acceptor is seen to bind to the active site of Cst-II through interactions primarily mediated by Asn-51, Tyr-81, and Arg-129. Kinetic and structural analyses of mutants modified at these positions indicate that these residues are critical for acceptor binding and catalysis, thereby providing significant new insight into the kinetic and catalytic mechanism and acceptor specificity of this pathogen encoded bifunctional GT-42 sialyltransferase.
Structural and kinetic analysis of substrate binding to the sialyltransferase CST-II from Campylobacter Jejuni.,Lee HJ, Lairson LL, Rich JR, Lameignere E, Wakarchuk WW, Withers SG, Strynadka NC J Biol Chem. 2011 Aug 8. PMID:21832050[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lee HJ, Lairson LL, Rich JR, Lameignere E, Wakarchuk WW, Withers SG, Strynadka NC. Structural and kinetic analysis of substrate binding to the sialyltransferase CST-II from Campylobacter Jejuni. J Biol Chem. 2011 Aug 8. PMID:21832050 doi:10.1074/jbc.M111.261172
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