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1wsz

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Revision as of 06:24, 20 May 2020

Mutant human ABO(H) blood group transferase A

Structural highlights

1wsz is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1lz0, 1wt0, 1wt1, 1wt2, 1wt3
Activity:	Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase, with EC number 2.4.1.40
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.

Publication Abstract from PubMed

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.

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:15475562^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lee HJ, Barry CH, Borisova SN, Seto NO, Zheng RB, Blancher A, Evans SV, Palcic MM. Structural basis for the inactivity of human blood group O2 glycosyltransferase. J Biol Chem. 2005 Jan 7;280(1):525-9. Epub 2004 Oct 8. PMID:15475562 doi:http://dx.doi.org/10.1074/jbc.M410245200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1wsz"

@@ Line 1: / Line 1: @@
 ==Mutant human ABO(H) blood group transferase A==
-<StructureSection load='1wsz' size='340' side='right' caption='[[1wsz]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
+<StructureSection load='1wsz' size='340' side='right'caption='[[1wsz]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1wsz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WSZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WSZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1wsz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WSZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1WSZ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lz0|1lz0]], [[1wt0|1wt0]], [[1wt1|1wt1]], [[1wt2|1wt2]], [[1wt3|1wt3]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wsz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wsz OCA], [http://pdbe.org/1wsz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wsz RCSB], [http://www.ebi.ac.uk/pdbsum/1wsz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wsz ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1wsz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wsz OCA], [http://pdbe.org/1wsz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wsz RCSB], [http://www.ebi.ac.uk/pdbsum/1wsz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wsz ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 32: / Line 32: @@
 ==See Also==
-*[[Glycosyltransferase|Glycosyltransferase]]
+*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
 == References ==
 <references/>
@@ Line 39: / Line 39: @@
 [[Category: Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase]]
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Barry, C H]]
 [[Category: Blancher, A]]

1wsz

From Proteopedia

Revision as of 06:24, 20 May 2020

Mutant human ABO(H) blood group transferase A

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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