2rj0: Difference between revisions

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==B-specific alpha-1,3-galactosyltransferase G176R mutant + UDP+ Mn2+==
The line below this paragraph, containing "STRUCTURE_2rj0", creates the "Structure Box" on the page.
<StructureSection load='2rj0' size='340' side='right'caption='[[2rj0]], [[Resolution|resolution]] 1.52&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2rj0]] 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=2RJ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RJ0 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.52&#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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
{{STRUCTURE_2rj0| PDB=2rj0 |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rj0 OCA], [https://pdbe.org/2rj0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rj0 RCSB], [https://www.ebi.ac.uk/pdbsum/2rj0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rj0 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/rj/2rj0_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=2rj0 ConSurf].
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'''B-specific alpha-1,3-galactosyltransferase G176R mutant + UDP+ Mn2+'''
==See Also==
 
*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The final step in the enzymatic synthesis of the ABO(H) blood group A and B antigens is catalyzed by two closely related glycosyltransferases, an a-(1-3)-N-acetylgalactosaminyltransferase (GTA) and an a-(1-3)-galactosyltransferase (GTB). Of their 354 amino acid residues, GTA and GTB differ by only four 'critical' residues. High-resolution structures for GTB and the GTA/GTB chimeric enzymes GTB/G176R and GTB/G176R/G235S bound to a panel of donor and acceptor analog substrates reveal 'open', 'semi-closed' and 'closed' conformations as the enzymes go from the unliganded to the liganded states. In the 'open' form the internal polypeptide loop (amino acid residues 177-195) adjacent to the active site in the unliganded or H-antigen-bound enzymes is composed of two a-helices spanning Arg180-Met186 and Arg188-Asp194 respectively. The 'semi-closed' and closed forms of the enzymes are generated by binding of UDP or of UDP and H-antigen analogs respectively, and show that these helices merge to form a single distorted helical structure with alternating a-310-a character that partially occludes the active site. The 'closed' form is distinguished from the 'semi-closed' form by the ordering of the final nine C-terminal residues through the formation of hydrogen bonds to both UDP and H-antigen analogs. The 'semi-closed' forms for various mutants generally show significantly more disorder than the 'open' forms, while the 'closed' forms display little or no disorder depending strongly on the identity of residue 176. Finally, the use of synthetic analogs reveals how H-antigen acceptor binding can be critical in stabilizing the 'closed' conformation. These structures demonstrate a delicately-balanced substrate recognition mechanism and give insight on critical aspects of donor and acceptor specificity, on the order of substrate binding, and on the requirements for catalysis.
 
==Disease==
Known disease associated with this structure: Blood group, ABO system OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=110300 110300]]
 
==About this Structure==
2RJ0 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=2RJ0 OCA].
 
==Reference==
ABO(H) blood group A and B glycosyltransferases recognize substrate via specific conformational changes., Alfaro JA, Zheng RB, Persson M, Letts JA, Polakowski R, Bai Y, Borisova SN, Seto NO, Lowary TL, Palcic MM, Evans SV, J Biol Chem. 2008 Jan 11;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18192272 18192272]
[[Category: Fucosylgalactoside 3-alpha-galactosyltransferase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Alfaro, J A.]]
[[Category: Alfaro JA]]
[[Category: Evans, S V.]]
[[Category: Evans SV]]
[[Category: Blood group antigen]]
[[Category: Glycoprotein]]
[[Category: Glycosyltransferase]]
[[Category: Golgi apparatus]]
[[Category: Gtb abo rossman fold abbb udp mn2+]]
[[Category: Manganese]]
[[Category: Membrane]]
[[Category: Metal-binding]]
[[Category: Polymorphism]]
[[Category: Secreted]]
[[Category: Signal-anchor]]
[[Category: Transferase]]
[[Category: Transmembrane]]
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