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[[ | ==CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE CST-II Y81F IN COMPLEX WITH CMP== | ||
<StructureSection load='2x62' size='340' side='right' caption='[[2x62]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2x62]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X62 OCA]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CH:N3-PROTONATED+CYTIDINE-5-MONOPHOSPHATE'>CH</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ro8|1ro8]], [[2x63|2x63]], [[1ro7|1ro7]], [[2x61|2x61]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2x62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x62 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2x62 RCSB], [http://www.ebi.ac.uk/pdbsum/2x62 PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:21832050</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Campylobacter jejuni]] | [[Category: Campylobacter jejuni]] | ||
[[Category: Lairson, L L.]] | [[Category: Lairson, L L.]] | ||
Revision as of 10:40, 14 May 2014
CRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE CST-II Y81F IN COMPLEX WITH CMPCRYSTAL STRUCTURE OF THE SIALYLTRANSFERASE CST-II Y81F IN COMPLEX WITH CMP
Structural highlights
Publication Abstract from PubMedSialic 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. References
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