2nzx: Difference between revisions

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==Crystal Structure of alpha1,3-Fucosyltransferase with GDP==

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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AF008596 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 ATCC 43504])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-galactosyl-N-acetylglucosaminide_3-alpha-L-fucosyltransferase 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.152 2.4.1.152] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nzx OCA], [http://pdbe.org/2nzx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nzx RCSB], [http://www.ebi.ac.uk/pdbsum/2nzx PDBsum]</span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nzx OCA], [http://pdbe.org/2nzx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nzx RCSB], [http://www.ebi.ac.uk/pdbsum/2nzx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2nzx ProSAT]</span></td></tr>

</table>

== Evolutionary Conservation ==

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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=2nzx ConSurf].

== 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>

== References ==

__TOC__

</StructureSection>

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 ==Crystal Structure of alpha1,3-Fucosyltransferase with GDP==
 <StructureSection load='2nzx' size='340' side='right' caption='[[2nzx]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AF008596 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 ATCC 43504])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-galactosyl-N-acetylglucosaminide_3-alpha-L-fucosyltransferase 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.152 2.4.1.152] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nzx OCA], [http://pdbe.org/2nzx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nzx RCSB], [http://www.ebi.ac.uk/pdbsum/2nzx PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nzx OCA], [http://pdbe.org/2nzx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nzx RCSB], [http://www.ebi.ac.uk/pdbsum/2nzx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2nzx ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 19: / Line 20: @@
 </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=2nzx 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2nzx" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>