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2nzw
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="2nzw" size="350" color="white" frame="true" align="right" spinBox="true" caption="2nzw, resolution 1.9Å" /> '''Crystal Structure of ...) |
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| - | [[Image:2nzw.gif|left|200px]]<br /><applet load="2nzw" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2nzw, resolution 1.9Å" /> | ||
| - | '''Crystal Structure of alpha1,3-Fucosyltransferase'''<br /> | ||
| - | == | + | ==Crystal Structure of alpha1,3-Fucosyltransferase== |
| - | + | <StructureSection load='2nzw' size='340' side='right'caption='[[2nzw]], [[Resolution|resolution]] 1.90Å' scene=''> | |
| - | [ | + | == Structural highlights == |
| - | [[ | + | <table><tr><td colspan='2'>[[2nzw]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NZW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NZW 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]] 1.9Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2nzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nzw OCA], [https://pdbe.org/2nzw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nzw RCSB], [https://www.ebi.ac.uk/pdbsum/2nzw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nzw ProSAT]</span></td></tr> |
| - | [[ | + | </table> |
| - | [ | + | == Function == |
| - | + | [https://www.uniprot.org/uniprot/FUCT_HELPX FUCT_HELPX] Involved in the biosynthesis of the Lewis X (LeX) trisaccharide of the lipopolysaccharide (LPS) O-antigen. Catalyzes the addition of fucose in alpha 1-3 linkage to Gal-beta-1-4-GlcNAc-beta-O-R (LacNAc-R) type II acceptor.<ref>PMID:12676935</ref> <ref>PMID:16150700</ref> <ref>PMID:16800635</ref> <ref>PMID:17251184</ref> <ref>PMID:9261149</ref> | |
| - | + | == 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/nz/2nzw_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2nzw ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Helicobacter pylori alpha1,3-fucosyltransferase (FucT) is involved in catalysis to produce the Lewis x trisaccharide, the major component of the bacteria's lipopolysaccharides, which has been suggested to mimic the surface sugars in gastric epithelium to escape host immune surveillance. We report here three x-ray crystal structures of FucT, including the FucT.GDP-fucose and FucT.GDP complexes. The protein structure is typical of the glycosyltransferase-B family despite little sequence homology. We identified a number of catalytically important residues, including Glu-95, which serves as the general base, and Glu-249, which stabilizes the developing oxonium ion during catalysis. The residues Arg-195, Tyr-246, Glu-249, and Lys-250 serve to interact with the donor substrate, GDP-fucose. Variations in the protein and ligand conformations, as well as a possible FucT dimer, were also observed. We propose a catalytic mechanism and a model of polysaccharide binding not only to explain the observed variations in H. pylori lipopolysaccharides, but also to facilitate the development of potent inhibitors. | ||
| - | + | Structure and mechanism of Helicobacter pylori fucosyltransferase. A basis for lipopolysaccharide variation and inhibitor design.,Sun HY, Lin SW, Ko TP, Pan JF, Liu CL, Lin CN, Wang AH, Lin CH J Biol Chem. 2007 Mar 30;282(13):9973-82. Epub 2007 Jan 24. PMID:17251184<ref>PMID:17251184</ref> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2nzw" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Helicobacter pylori]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ko TP]] | ||
| + | [[Category: Sun HY]] | ||
Current revision
Crystal Structure of alpha1,3-Fucosyltransferase
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