1lzi: Difference between revisions

New page: left|200px<br /> <applet load="1lzi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lzi, resolution 1.35Å" /> '''Glycosyltransferase...
 
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[[Image:1lzi.gif|left|200px]]<br />
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'''Glycosyltransferase A + UDP + H antigen acceptor'''<br />


==Overview==
==Glycosyltransferase A + UDP + H antigen acceptor==
The human ABO(H) blood group antigens are produced by specific, glycosyltransferase enzymes. An N-acetylgalactosaminyltransferase (GTA), uses a UDP-GalNAc donor to convert the H-antigen acceptor to the A, antigen, whereas a galactosyltransferase (GTB) uses a UDP-galactose donor, to convert the H-antigen acceptor to the B antigen. GTA and GTB differ, only in the identity of four critical amino acid residues. Crystal, structures at 1.8-1.32 A resolution of the GTA and GTB enzymes both free, and in complex with disaccharide H-antigen acceptor and UDP reveal the, basis for donor and acceptor specificity and show that only two of the, critical amino acid residues are positioned to contact donor or acceptor, substrates. Given the need for stringent stereo- and regioselectivity in, this biosynthesis, these structures further demonstrate that the ability, of the two enzymes to distinguish between the A and B donors is largely, determined by a single amino acid residue.
<StructureSection load='1lzi' size='340' side='right'caption='[[1lzi]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1lzi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The December 2012 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''ABO Blood Type Glycosyltransferases''  by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2012_12 10.2210/rcsb_pdb/mom_2012_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LZI 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]] 1.35&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BHG:2-HEXYLOXY-6-HYDROXYMETHYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL'>BHG</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <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=1lzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lzi OCA], [https://pdbe.org/1lzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lzi RCSB], [https://www.ebi.ac.uk/pdbsum/1lzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lzi 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/lz/1lzi_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=1lzi ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The human ABO(H) blood group antigens are produced by specific glycosyltransferase enzymes. An N-acetylgalactosaminyltransferase (GTA) uses a UDP-GalNAc donor to convert the H-antigen acceptor to the A antigen, whereas a galactosyltransferase (GTB) uses a UDP-galactose donor to convert the H-antigen acceptor to the B antigen. GTA and GTB differ only in the identity of four critical amino acid residues. Crystal structures at 1.8-1.32 A resolution of the GTA and GTB enzymes both free and in complex with disaccharide H-antigen acceptor and UDP reveal the basis for donor and acceptor specificity and show that only two of the critical amino acid residues are positioned to contact donor or acceptor substrates. Given the need for stringent stereo- and regioselectivity in this biosynthesis, these structures further demonstrate that the ability of the two enzymes to distinguish between the A and B donors is largely determined by a single amino acid residue.


==Disease==
The structural basis for specificity in human ABO(H) blood group biosynthesis.,Patenaude SI, Seto NO, Borisova SN, Szpacenko A, Marcus SL, Palcic MM, Evans SV Nat Struct Biol. 2002 Sep;9(9):685-90. PMID:12198488<ref>PMID:12198488</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1LZI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with HG, MN and UDP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glycoprotein-fucosylgalactoside_alpha-N-acetylgalactosaminyltransferase Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.40 2.4.1.40] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LZI OCA].
</div>
<div class="pdbe-citations 1lzi" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
The structural basis for specificity in human ABO(H) blood group biosynthesis., Patenaude SI, Seto NO, Borisova SN, Szpacenko A, Marcus SL, Palcic MM, Evans SV, Nat Struct Biol. 2002 Sep;9(9):685-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12198488 12198488]
*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
[[Category: Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: ABO Blood Type Glycosyltransferases]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Borisova, S.N.]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Evans, S.V.]]
[[Category: Borisova SN]]
[[Category: Marcus, S.L.]]
[[Category: Evans SV]]
[[Category: Palcic, M.M.]]
[[Category: Marcus SL]]
[[Category: Patenaude, S.I.]]
[[Category: Palcic MM]]
[[Category: Seto, N.O.L.]]
[[Category: Patenaude SI]]
[[Category: Szpacenko, A.]]
[[Category: Seto NOL]]
[[Category: HG]]
[[Category: Szpacenko A]]
[[Category: MN]]
[[Category: UDP]]
[[Category: blood group antigen]]
[[Category: glycoprotein]]
[[Category: signal-anchor]]
[[Category: transmembrane]]
 
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