1wt3: Difference between revisions

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New page: left|200px<br /> <applet load="1wt3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wt3, resolution 1.8Å" /> '''Mutant human ABO(H) ...
 
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[[Image:1wt3.gif|left|200px]]<br />
<applet load="1wt3" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1wt3, resolution 1.8&Aring;" />
'''Mutant human ABO(H) blood group glycosyltransferase with bound UDP and acceptor'''<br />


==Overview==
==Mutant human ABO(H) blood group glycosyltransferase with bound UDP and acceptor==
The human ABO(H) blood group antigens are carbohydrate structures, generated by glycosyltransferase enzymes. Glycosyltransferase A (GTA) uses, UDP-GalNAc as a donor to transfer a monosaccharide residue to Fuc, alpha1-2Gal beta-R (H)-terminating acceptors. Similarly, glycosyltransferase B (GTB) catalyzes the transfer of a monosaccharide, residue from UDP-Gal to the same acceptors. These are highly homologous, enzymes differing in only four of 354 amino acids, Arg/Gly-176, Gly/Ser-235, Leu/Met-266, and Gly/Ala-268. Blood group O usually stems, from the expression of truncated inactive forms of GTA or GTB. Recently, an O(2) enzyme was discovered that was a full-length form of GTA with, three mutations, P74S, R176G, and G268R. We showed previously that the, R176G mutation increased catalytic activity with minor effects on, substrate binding. Enzyme kinetics and high resolution structural studies, of mutant enzymes based on the O(2) blood group transferase reveal that, whereas the P74S mutation in the stem region of the protein does not, appear to play a role in enzyme inactivation, the G268R mutation, completely blocks the donor GalNAc-binding site leaving the acceptor, binding site unaffected.
<StructureSection load='1wt3' size='340' side='right'caption='[[1wt3]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1wt3]] 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=1WT3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WT3 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]] 1.8&#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=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=1wt3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wt3 OCA], [https://pdbe.org/1wt3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wt3 RCSB], [https://www.ebi.ac.uk/pdbsum/1wt3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wt3 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/wt/1wt3_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=1wt3 ConSurf].
<div style="clear:both"></div>


==Disease==
==See Also==
Known disease associated with this structure: Blood group, ABO system OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=110300 110300]]
*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
 
__TOC__
==About this Structure==
</StructureSection>
1WT3 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 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=1WT3 OCA].
 
==Reference==
Structural basis for the inactivity of human blood group O2 glycosyltransferase., Lee HJ, Barry CH, Borisova SN, Seto NO, Zheng RB, Blancher A, Evans SV, Palcic MM, J Biol Chem. 2005 Jan 7;280(1):525-9. Epub 2004 Oct 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15475562 15475562]
[[Category: Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Barry, C.H.]]
[[Category: Barry CH]]
[[Category: Blancher, A.]]
[[Category: Blancher A]]
[[Category: Borisova, S.N.]]
[[Category: Borisova SN]]
[[Category: Evans, S.V.]]
[[Category: Evans SV]]
[[Category: Lee, H.J.]]
[[Category: Lee HJ]]
[[Category: Palcic, M.M.]]
[[Category: Palcic MM]]
[[Category: Seto, N.O.L.]]
[[Category: Seto NOL]]
[[Category: Zheng, R.B.]]
[[Category: Zheng RB]]
[[Category: HG]]
[[Category: UDP]]
[[Category: transferase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:54:42 2007''

Latest revision as of 16:34, 13 March 2024

Mutant human ABO(H) blood group glycosyltransferase with bound UDP and acceptorMutant human ABO(H) blood group glycosyltransferase with bound UDP and acceptor

Structural highlights

1wt3 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1wt3, resolution 1.80Å

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