1lz7: Difference between revisions
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|PDB= 1lz7 |SIZE=350|CAPTION= <scene name='initialview01'>1lz7</scene>, resolution 1.65Å | |PDB= 1lz7 |SIZE=350|CAPTION= <scene name='initialview01'>1lz7</scene>, resolution 1.65Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=HG:MERCURY (II) ION'>HG</scene> | |LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1lz0|1LZ0]], [[1lzi|1LZI]], [[1lzj|1LZJ]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lz7 OCA], [http://www.ebi.ac.uk/pdbsum/1lz7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lz7 RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
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. | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Seto, N O.L.]] | [[Category: Seto, N O.L.]] | ||
[[Category: Szpacenko, A.]] | [[Category: Szpacenko, A.]] | ||
[[Category: blood group antigen]] | [[Category: blood group antigen]] | ||
[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:09:11 2008'' | ||
Revision as of 22:09, 30 March 2008
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| , resolution 1.65Å | |||||||
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| Ligands: | |||||||
| Related: | 1LZ0, 1LZI, 1LZJ
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Glycosyltransferase B
OverviewOverview
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.
About this StructureAbout this Structure
1LZ7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
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