1ro7

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(New page: 200px<br /><applet load="1ro7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ro7, resolution 1.80&Aring;" /> '''Structural analysis ...)
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[[Image:1ro7.gif|left|200px]]<br /><applet load="1ro7" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ro7, resolution 1.80&Aring;" />
 
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'''Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analogue, CMP-3FNeuAc.'''<br />
 
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==Overview==
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==Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analogue, CMP-3FNeuAc.==
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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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<StructureSection load='1ro7' size='340' side='right'caption='[[1ro7]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9LAK3_CAMJU Q9LAK3_CAMJU]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ro/1ro7_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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==About this Structure==
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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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1RO7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni] with CSF and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RO7 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14730352 14730352]
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</div>
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[[Category: Campylobacter jejuni]]
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<div class="pdbe-citations 1ro7" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Chiu, C.P.]]
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[[Category: Gilbert, M.]]
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[[Category: Lairson, L.L.]]
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[[Category: Lim, D.]]
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[[Category: Strynadka, N.C.]]
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[[Category: Wakarchuk, W.W.]]
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[[Category: Watts, A.G.]]
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[[Category: Withers, S.G.]]
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[[Category: CSF]]
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[[Category: MPD]]
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[[Category: mixed alpha/beta]]
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[[Category: rossmann fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:00:55 2007''
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==See Also==
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*[[Sialyltransferase 3D structures|Sialyltransferase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Campylobacter jejuni]]
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[[Category: Large Structures]]
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[[Category: Chiu CP]]
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[[Category: Gilbert M]]
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[[Category: Lairson LL]]
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[[Category: Lim D]]
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[[Category: Strynadka NC]]
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[[Category: Wakarchuk WW]]
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[[Category: Watts AG]]
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[[Category: Withers SG]]

Current revision

Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analogue, CMP-3FNeuAc.

PDB ID 1ro7

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