1LZI

Glycosyltransferase A + UDP + H antigen acceptor

Summary for 1LZI

• Entry DOI: 10.2210/pdb1lzi/pdb
• Related: 1LZ0 1LZ7 1LZJ
• Descriptor: Glycosyltransferase A, alpha-L-fucopyranose-(1-2)-hexyl beta-D-galactopyranoside, MERCURY (II) ION, ... (6 entities in total)
• Functional Keywords: glycoprotein, transmembrane, signal-anchor, blood group antigen, transferase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 35919.83

Authors

Patenaude, S.I.,Seto, N.O.L.,Borisova, S.N.,Szpacenko, A.,Marcus, S.L.,Palcic, M.M.,Evans, S.V. (deposition date: 2002-06-10, release date: 2002-08-28, Last modification date: 2024-05-22)

Primary citation

Patenaude, S.I.,Seto, N.O.,Borisova, S.N.,Szpacenko, A.,Marcus, S.L.,Palcic, M.M.,Evans, S.V.
The structural basis for specificity in human ABO(H) blood group biosynthesis.
Nat.Struct.Biol., 9:685-690, 2002

PubMed Abstract: 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.

PubMed: 12198488
DOI: 10.1038/nsb832

Experimental method

X-RAY DIFFRACTION (1.35 Å)