2x61: Difference between revisions
New page: '''Unreleased structure''' The entry 2x61 is ON HOLD Authors: LEE, H.J., RICH, J.R., WAKARCHUK, W.W., WITHERS, S.G., STRYNADKA, N.C.J. Description: CRYSTAL STRUCTURE OF THE SIALYLTRANS... |
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The | ==Crystal structure of the sialyltransferase CST-II in complex with trisaccharide acceptor and CMP== | ||
<StructureSection load='2x61' size='340' side='right'caption='[[2x61]], [[Resolution|resolution]] 1.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2x61]] is a 2 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=2X61 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X61 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CH:N3-PROTONATED+CYTIDINE-5-MONOPHOSPHATE'>CH</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NGA:N-ACETYL-D-GALACTOSAMINE'>NGA</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></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=2x61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x61 OCA], [https://pdbe.org/2x61 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x61 RCSB], [https://www.ebi.ac.uk/pdbsum/2x61 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x61 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9LAK3_CAMJU Q9LAK3_CAMJU] | |||
<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> | |||
<div class="pdbe-citations 2x61" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Sialyltransferase|Sialyltransferase]] | |||
*[[Sialyltransferase 3D structures|Sialyltransferase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Campylobacter jejuni]] | |||
[[Category: Large Structures]] | |||
[[Category: Lairson LL]] | |||
[[Category: Lee HJ]] | |||
[[Category: Rich JR]] | |||
[[Category: Strynadka NCJ]] | |||
[[Category: Wakarchuk WW]] | |||
[[Category: Withers SG]] | |||
Latest revision as of 13:24, 20 December 2023
Crystal structure of the sialyltransferase CST-II in complex with trisaccharide acceptor and CMPCrystal structure of the sialyltransferase CST-II in complex with trisaccharide acceptor and CMP
Structural highlights
FunctionPublication 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. See AlsoReferences
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