1ro7
From Proteopedia
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<StructureSection load='1ro7' size='340' side='right'caption='[[1ro7]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1ro7' size='340' side='right'caption='[[1ro7]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1ro7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1ro7]] is a 4 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=1RO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RO7 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSF:CYTIDINE-5-MONOPHOSPHATE-3-FLUORO-N-ACETYL-NEURAMINIC+ACID'>CSF</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ro7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ro7 OCA], [https://pdbe.org/1ro7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ro7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ro7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ro7 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=1ro7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ro7 OCA], [https://pdbe.org/1ro7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ro7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ro7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ro7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q9LAK3_CAMJU Q9LAK3_CAMJU] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=1ro7 ConSurf]. | </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=1ro7 ConSurf]. | ||
<div style="clear:both"></div> | <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. | ||
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| - | 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 1ro7" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Sialyltransferase 3D structures|Sialyltransferase 3D structures]] | *[[Sialyltransferase 3D structures|Sialyltransferase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Campylobacter | + | [[Category: Campylobacter jejuni]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Chiu | + | [[Category: Chiu CP]] |
| - | [[Category: Gilbert | + | [[Category: Gilbert M]] |
| - | [[Category: Lairson | + | [[Category: Lairson LL]] |
| - | [[Category: Lim | + | [[Category: Lim D]] |
| - | [[Category: Strynadka | + | [[Category: Strynadka NC]] |
| - | [[Category: Wakarchuk | + | [[Category: Wakarchuk WW]] |
| - | [[Category: Watts | + | [[Category: Watts AG]] |
| - | [[Category: Withers | + | [[Category: Withers SG]] |
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Revision as of 08:25, 1 May 2024
Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analogue, CMP-3FNeuAc.
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