2a8u: Difference between revisions

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-[[Image:2a8u.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_2a8u", creates the "Structure Box" on the page.
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-{{STRUCTURE_2a8u|  PDB=2a8u  |  SCENE=  }}
-'''Crystal Structure of Human Galactosyltransferase (GTB) Complexed with Beta-Methyl Lactoside'''
+==Crystal Structure of Human Galactosyltransferase (GTB) Complexed with Beta-Methyl Lactoside==
+<StructureSection load='2a8u' size='340' side='right'caption='[[2a8u]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2a8u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A8U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A8U 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]] 1.69&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=MGL:O1-METHYL-GLUCOSE'>MGL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PRD_900076:Beta-Methyl+Lactoside'>PRD_900076</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</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=2a8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a8u OCA], [https://pdbe.org/2a8u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a8u RCSB], [https://www.ebi.ac.uk/pdbsum/2a8u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a8u ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/BGAT_HUMAN BGAT_HUMAN] This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity.
+== 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/a8/2a8u_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=2a8u ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The human ABO(H) blood group A and B antigens are generated by the homologous glycosyltransferases A (GTA) and B (GTB), which add the monosaccharides GalNAc and Gal, respectively, to the cell-surface H antigens. In the first comprehensive structural study of the recognition by a glycosyltransferase of a panel of substrates corresponding to acceptor fragments, 14 high resolution crystal structures of GTA and GTB have been determined in the presence of oligosaccharides corresponding to different segments of the type I (alpha-l-Fucp-(1--&gt;2)-beta-D-Galp-(1--&gt;3)-beta-D-GlcNAcp-OR, where R is a glycoprotein or glycolipid in natural acceptors) and type II (alpha-l-Fucp-(1--&gt;2)-beta-D-Galp-(1--&gt;4)-beta-d-GlcNAcp-OR) H antigen trisaccharides. GTA and GTB differ in only four "critical" amino acid residues (Arg/Gly-176, Gly/Ser-235, Leu/Met-266, and Gly/Ala-268). As these enzymes both utilize the H antigen acceptors, the four critical residues had been thought to be involved strictly in donor recognition; however, we now report that acceptor binding and subsequent transfer are significantly influenced by two of these residues: Gly/Ser-235 and Leu/Met-266. Furthermore, these structures show that acceptor recognition is dominated by the central Gal residue despite the fact that the L-Fuc residue is required for efficient catalysis and give direct insight into the design of model inhibitors for GTA and GTB.
-==Overview==
+Differential recognition of the type I and II H antigen acceptors by the human ABO(H) blood group A and B glycosyltransferases.,Letts JA, Rose NL, Fang YR, Barry CH, Borisova SN, Seto NO, Palcic MM, Evans SV J Biol Chem. 2006 Feb 10;281(6):3625-32. Epub 2005 Dec 2. PMID:16326711<ref>PMID:16326711</ref>
-The human ABO(H) blood group A and B antigens are generated by the homologous glycosyltransferases A (GTA) and B (GTB), which add the monosaccharides GalNAc and Gal, respectively, to the cell-surface H antigens. In the first comprehensive structural study of the recognition by a glycosyltransferase of a panel of substrates corresponding to acceptor fragments, 14 high resolution crystal structures of GTA and GTB have been determined in the presence of oligosaccharides corresponding to different segments of the type I (alpha-l-Fucp-(1--&gt;2)-beta-D-Galp-(1--&gt;3)-beta-D-GlcNAcp-OR, where R is a glycoprotein or glycolipid in natural acceptors) and type II (alpha-l-Fucp-(1--&gt;2)-beta-D-Galp-(1--&gt;4)-beta-d-GlcNAcp-OR) H antigen trisaccharides. GTA and GTB differ in only four "critical" amino acid residues (Arg/Gly-176, Gly/Ser-235, Leu/Met-266, and Gly/Ala-268). As these enzymes both utilize the H antigen acceptors, the four critical residues had been thought to be involved strictly in donor recognition; however, we now report that acceptor binding and subsequent transfer are significantly influenced by two of these residues: Gly/Ser-235 and Leu/Met-266. Furthermore, these structures show that acceptor recognition is dominated by the central Gal residue despite the fact that the L-Fuc residue is required for efficient catalysis and give direct insight into the design of model inhibitors for GTA and GTB.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-A8U is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A8U OCA].
+</div>
+<div class="pdbe-citations 2a8u" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Differential recognition of the type I and II H antigen acceptors by the human ABO(H) blood group A and B glycosyltransferases., Letts JA, Rose NL, Fang YR, Barry CH, Borisova SN, Seto NO, Palcic MM, Evans SV, J Biol Chem. 2006 Feb 10;281(6):3625-32. Epub 2005 Dec 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16326711 16326711]
+*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Barry, C H.]]
+[[Category: Barry CH]]
-[[Category: Borisova, S N.]]
+[[Category: Borisova SN]]
-[[Category: Evans, S V.]]
+[[Category: Evans SV]]
-[[Category: Fang, Y R.]]
+[[Category: Fang YR]]
-[[Category: Letts, J A.]]
+[[Category: Letts JA]]
-[[Category: Palcic, M M.]]
+[[Category: Palcic MM]]
-[[Category: Rose, N L.]]
+[[Category: Rose NL]]
-[[Category: Seto, N O.]]
+[[Category: Seto NO]]
-[[Category: Blood group]]
-[[Category: Glycosyltransferase]]
-[[Category: Gtb]]
-[[Category: Retaining]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:45:19 2008''