2y7a

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Current revision (10:47, 20 December 2023) (edit) (undo)
 
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<StructureSection load='2y7a' size='340' side='right'caption='[[2y7a]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
<StructureSection load='2y7a' size='340' side='right'caption='[[2y7a]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2y7a]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y7A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y7A FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2y7a]] is a 4 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=2Y7A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y7A FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
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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]] 2.06&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Fucosylgalactoside_3-alpha-galactosyltransferase Fucosylgalactoside 3-alpha-galactosyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.37 2.4.1.37] </span></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=MN:MANGANESE+(II)+ION'>MN</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=2y7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y7a OCA], [https://pdbe.org/2y7a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y7a RCSB], [https://www.ebi.ac.uk/pdbsum/2y7a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y7a 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=2y7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y7a OCA], [https://pdbe.org/2y7a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y7a RCSB], [https://www.ebi.ac.uk/pdbsum/2y7a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y7a ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[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.
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A common feature in the structures of GT-A-fold-type glycosyltransferases is a mobile polypeptide loop that has been observed to participate in substrate recognition and enclose the active site upon substrate binding. This is the case for the human ABO(H) blood group B glycosyltransferase GTB, where amino acid residues 177-195 display significantly higher levels of disorder in the unliganded state than in the fully liganded state. Structural studies of mutant enzymes GTB/C80S/C196S and GTB/C80S/C196S/C209S at resolutions ranging from 1.93 to 1.40 A display the opposite trend, where the unliganded structures show nearly complete ordering of the mobile loop residues that is lost upon substrate binding. In the liganded states of the mutant structures, while the UDP moiety of the donor molecule is observed to bind in the expected location, the galactose moiety is observed to bind in a conformation significantly different from that observed for the wild-type chimeric structures. Although this would be expected to impede catalytic turnover, the kinetics of the transfer reaction are largely unaffected. These structures demonstrate that the enzymes bind the donor in a conformation more similar to the dominant solution rotamer and facilitate its gyration into the catalytically competent form. Further, by preventing active-site closure, these structures provide a basis for recently observed cooperativity in substrate binding. Finally, the mutation of C80S introduces a fully occupied UDP binding site at the enzyme dimer interface that is observed to be dependent on the binding of H antigen acceptor analog.
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Cysteine-to-serine mutants dramatically reorder the active site of human ABO(H) blood group B glycosyltransferase without affecting activity: structural insights into cooperative substrate binding.,Schuman B, Persson M, Landry RC, Polakowski R, Weadge JT, Seto NO, Borisova SN, Palcic MM, Evans SV J Mol Biol. 2010 Sep 17;402(2):399-411. Epub 2010 Jul 23. PMID:20655926<ref>PMID:20655926</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2y7a" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Fucosylgalactoside 3-alpha-galactosyltransferase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Henriksen, A]]
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[[Category: Henriksen A]]
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[[Category: Palcic, M M]]
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[[Category: Palcic MM]]
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[[Category: Weadge, J]]
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[[Category: Weadge J]]
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[[Category: Abo blood group]]
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[[Category: Transferase]]
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Current revision

Crystal structure of unliganded GTB P156L

PDB ID 2y7a

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OCA

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