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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 9 685-90 (2002)
Related entries: 1lz7, 1lzi, 1lzj

Cited: 122 times
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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.

Articles - 1lz0 mentioned but not cited (3)

  1. ABO exon and intron analysis in individuals with the AweakB phenotype reveals a novel O1v-A2 hybrid allele that causes four missense mutations in the A transferase. Hosseini-Maaf B, Hellberg A, Rodrigues MJ, Chester MA, Olsson ML. BMC Genet 4 17 (2003)
  2. High Resolution Structures of the Human ABO(H) Blood Group Enzymes in Complex with Donor Analogs Reveal That the Enzymes Utilize Multiple Donor Conformations to Bind Substrates in a Stepwise Manner. Gagnon SML, Meloncelli PJ, Zheng RB, Haji-Ghassemi O, Johal AR, Borisova SN, Lowary TL, Evans SV. J Biol Chem 290 27040-27052 (2015)
  3. Conserved residues Arg188 and Asp302 are critical for active site organization and catalysis in human ABO(H) blood group A and B glycosyltransferases. Gagnon SML, Legg MSG, Polakowski R, Letts JA, Persson M, Lin S, Zheng RB, Rempel B, Schuman B, Haji-Ghassemi O, Borisova SN, Palcic MM, Evans SV. Glycobiology 28 624-636 (2018)


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  19. Computer Simulation to Rationalize "Rational" Engineering of Glycoside Hydrolases and Glycosyltransferases. Coines J, Cuxart I, Teze D, Rovira C. J Phys Chem B 126 802-812 (2022)
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  21. Beyond history and "on a roll": The list of the most well-studied human protein structures and overall trends in the protein data bank. Li ZL, Buck M. Protein Sci 30 745-760 (2021)
  22. Identification of Regulatory Molecular "Hot Spots" for LH/PLOD Collagen Glycosyltransferase Activity. Mattoteia D, Chiapparino A, Fumagalli M, De Marco M, De Giorgi F, Negro L, Pinnola A, Faravelli S, Roscioli T, Scietti L, Forneris F. Int J Mol Sci 24 11213 (2023)
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