1ro8
From Proteopedia
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| - | [[Image:1ro8.gif|left|200px]]<br /><applet load="1ro8" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1ro8, resolution 2.05Å" /> | ||
| - | '''Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analogue, cytidine-5'-monophosphate'''<br /> | ||
| - | == | + | ==Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analogue, cytidine-5'-monophosphate== |
| + | <StructureSection load='1ro8' size='340' side='right'caption='[[1ro8]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1ro8]] 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=1RO8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RO8 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]] 2.05Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C5P:CYTIDINE-5-MONOPHOSPHATE'>C5P</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1ro8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ro8 OCA], [https://pdbe.org/1ro8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ro8 RCSB], [https://www.ebi.ac.uk/pdbsum/1ro8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ro8 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q9LAK3_CAMJU Q9LAK3_CAMJU] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ro/1ro8_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ro8 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Sialic acid terminates oligosaccharide chains on mammalian and microbial cell surfaces, playing critical roles in recognition and adherence. The enzymes that transfer the sialic acid moiety from cytidine-5'-monophospho-N-acetyl-neuraminic acid (CMP-NeuAc) to the terminal positions of these key glycoconjugates are known as sialyltransferases. Despite their important biological roles, little is understood about the mechanism or molecular structure of these membrane-associated enzymes. We report the first structure of a sialyltransferase, that of CstII from Campylobacter jejuni, a highly prevalent foodborne pathogen. Our structural, mutagenesis and kinetic data provide support for a novel mode of substrate binding and glycosyl transfer mechanism, including essential roles of a histidine (general base) and two tyrosine residues (coordination of the phosphate leaving group). This work provides a framework for understanding the activity of several sialyltransferases, from bacterial to human, and for the structure-based design of specific inhibitors. | Sialic acid terminates oligosaccharide chains on mammalian and microbial cell surfaces, playing critical roles in recognition and adherence. The enzymes that transfer the sialic acid moiety from cytidine-5'-monophospho-N-acetyl-neuraminic acid (CMP-NeuAc) to the terminal positions of these key glycoconjugates are known as sialyltransferases. Despite their important biological roles, little is understood about the mechanism or molecular structure of these membrane-associated enzymes. We report the first structure of a sialyltransferase, that of CstII from Campylobacter jejuni, a highly prevalent foodborne pathogen. Our structural, mutagenesis and kinetic data provide support for a novel mode of substrate binding and glycosyl transfer mechanism, including essential roles of a histidine (general base) and two tyrosine residues (coordination of the phosphate leaving group). This work provides a framework for understanding the activity of several sialyltransferases, from bacterial to human, and for the structure-based design of specific inhibitors. | ||
| - | + | Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analog.,Chiu CP, Watts AG, Lairson LL, Gilbert M, Lim D, Wakarchuk WW, Withers SG, Strynadka NC Nat Struct Mol Biol. 2004 Feb;11(2):163-70. Epub 2004 Jan 18. PMID:14730352<ref>PMID:14730352</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1ro8" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Sialyltransferase 3D structures|Sialyltransferase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Campylobacter jejuni]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chiu CP]] | ||
| + | [[Category: Gilbert M]] | ||
| + | [[Category: Lairson LL]] | ||
| + | [[Category: Lim D]] | ||
| + | [[Category: Strynadka NC]] | ||
| + | [[Category: Wakarchuk WW]] | ||
| + | [[Category: Watts AG]] | ||
| + | [[Category: Withers SG]] | ||
Current revision
Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analogue, cytidine-5'-monophosphate
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