PDBsum entry 1xz6

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protein metals links
Transferase PDB id
Protein chain
263 a.a. *
_HG ×4
Waters ×247
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Mutant abo(h) blood group glycosyltransferase a
Structure: Histo-blood group abo system transferase. Chain: a. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: abo. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PQS)
1.55Å     R-factor:   0.209     R-free:   0.243
Authors: H.J.Lee,C.H.Barry,S.N.Borisova,N.O.L.Seto,R.B.Zheng,A.Blanch S.V.Evans,M.M.Palcic
Key ref:
H.J.Lee et al. (2005). Structural basis for the inactivity of human blood group O2 glycosyltransferase. J Biol Chem, 280, 525-529. PubMed id: 15475562 DOI: 10.1074/jbc.M500897200
11-Nov-04     Release date:   07-Dec-04    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P16442  (BGAT_HUMAN) -  Histo-blood group ABO system transferase
354 a.a.
263 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 1: E.C.  - Fucosylgalactoside 3-alpha-galactosyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: UDP-alpha-D-galactose + alpha-L-fucosyl-(1->2)-D-galactosyl-R = UDP + alpha-D-galactosyl-(1->3)-(alpha-L-fucosyl-(1->2))-D-galactosyl-R
+ alpha-L-fucosyl-(1->2)-D-galactosyl-R
+ alpha-D-galactosyl-(1->3)-(alpha-L-fucosyl-(1->2))-D-galactosyl-R
   Enzyme class 2: E.C.  - Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: UDP-N-acetyl-alpha-beta-D-galactosamine + glycoprotein-alpha-L-fucosyl- (1->2)-D-galactose = UDP + glycoprotein-N-acetyl-alpha-D-galactosaminyl- (1->3)-(alpha-L-fucosyl-(1->2))-beta-D-galactose
+ glycoprotein-alpha-L-fucosyl- (1->2)-D-galactose
+ glycoprotein-N-acetyl-alpha-D-galactosaminyl- (1->3)-(alpha-L-fucosyl-(1->2))-beta-D-galactose
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   1 term 
  Biological process     carbohydrate metabolic process   1 term 
  Biochemical function     transferase activity, transferring hexosyl groups     1 term  


DOI no: 10.1074/jbc.M500897200 J Biol Chem 280:525-529 (2005)
PubMed id: 15475562  
Structural basis for the inactivity of human blood group O2 glycosyltransferase.
H.J.Lee, C.H.Barry, S.N.Borisova, N.O.Seto, R.B.Zheng, A.Blancher, S.V.Evans, M.M.Palcic.
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.
  Selected figure(s)  
Figure 1.
FIG. 1. Active site of the O2 glycosyltransferase triple mutant showing the observed electron density in the active site of the unliganded enzyme with ordered Arg-268 side chain (a), and the enzyme crystallized in the presence of the native H antigen acceptor that causes the Arg-268 and Leu-266 side chains to become disordered (b).
Figure 2.
FIG. 2. Overlap of the unliganded O2 enzyme showing Arg-268 and adjacent residues with the observed position of acceptor (green) and UDP (magenta) of wild-type GTA. The position of the GalNAc residue (magenta) has been modeled after Patenaude et al. (6) and shows severe conflicts with the Arg-268 side chain that completely blocks the sugar residue from the active site.
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2005, 280, 525-529) copyright 2005.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20655926 B.Schuman, M.Persson, R.C.Landry, R.Polakowski, J.T.Weadge, N.O.Seto, S.N.Borisova, M.M.Palcic, and S.V.Evans (2010).
Cysteine-to-serine mutants dramatically reorder the active site of human ABO(H) blood group B glycosyltransferase without affecting activity: structural insights into cooperative substrate binding.
  J Mol Biol, 402, 399-411.
PDB codes: 3i0c 3i0d 3i0e 3i0f 3i0g 3i0h 3i0i 3i0j 3i0k 3i0l
20533908 M.Kveiborg, J.Jacobsen, M.H.Lee, H.Nagase, U.M.Wewer, and G.Murphy (2010).
Selective inhibition of ADAM12 catalytic activity through engineering of tissue inhibitor of metalloproteinase 2 (TIMP-2).
  Biochem J, 430, 79-86.  
20030628 R.Hurtado-Guerrero, T.Zusman, S.Pathak, A.F.Ibrahim, S.Shepherd, A.Prescott, G.Segal, and D.M.van Aalten (2010).
Molecular mechanism of elongation factor 1A inhibition by a Legionella pneumophila glycosyltransferase.
  Biochem J, 426, 281-292.
PDB codes: 2wzf 2wzg
20306114 R.Weinlich, T.Brunner, and G.P.Amarante-Mendes (2010).
Control of death receptor ligand activity by posttranslational modifications.
  Cell Mol Life Sci, 67, 1631-1642.  
18630988 D.Christiansen, J.Milland, E.Mouhtouris, H.Vaughan, D.G.Pellicci, M.J.McConville, D.I.Godfrey, and M.S.Sandrin (2008).
Humans lack iGb3 due to the absence of functional iGb3-synthase: implications for NKT cell development and transplantation.
  PLoS Biol, 6, e172.  
18518825 L.L.Lairson, B.Henrissat, G.J.Davies, and S.G.Withers (2008).
Glycosyltransferases: structures, functions, and mechanisms.
  Annu Rev Biochem, 77, 521-555.  
18482182 M.H.Yazer, A.K.Hult, A.Hellberg, B.Hosseini-Maaf, M.M.Palcic, and M.L.Olsson (2008).
Investigation into A antigen expression on O2 heterozygous group O-labeled red blood cell units.
  Transfusion, 48, 1650-1657.  
18832934 M.H.Yazer, B.Hosseini-Maaf, and M.L.Olsson (2008).
Blood grouping discrepancies between ABO genotype and phenotype caused by O alleles.
  Curr Opin Hematol, 15, 618-624.  
18688480 T.Pesnot, and G.K.Wagner (2008).
Novel derivatives of UDP-glucose: concise synthesis and fluorescent properties.
  Org Biomol Chem, 6, 2884-2891.  
17465952 B.Hosseini-Maaf, J.A.Letts, M.Persson, E.Smart, P.Y.LePennec, H.Hustinx, Z.Zhao, M.M.Palcic, S.V.Evans, M.A.Chester, and M.L.Olsson (2007).
Structural basis for red cell phenotypic changes in newly identified, naturally occurring subgroup mutants of the human blood group B glycosyltransferase.
  Transfusion, 47, 864-875.
PDB code: 2i7b
16533287 A.Seltsam, C.Das Gupta, C.Bade-Doeding, and R.Blasczyk (2006).
A weak blood group A phenotype caused by a translation-initiator mutation in the ABO gene.
  Transfusion, 46, 434-440.  
16181218 A.Seltsam, and R.Blasczyk (2005).
Missense mutations outside the catalytic domain of the ABO glycosyltransferase can cause weak blood group A and B phenotypes.
  Transfusion, 45, 1663-1669.  
15987364 M.H.Yazer, G.A.Denomme, N.L.Rose, and M.M.Palcic (2005).
Amino-acid substitution in the disordered loop of blood group B-glycosyltransferase enzyme causes weak B phenotype.
  Transfusion, 45, 1178-1182.  
16202060 M.L.Olsson, B.Michalewska, A.Hellberg, A.Walaszczyk, and M.A.Chester (2005).
A clue to the basis of allelic enhancement: occurrence of the Ax subgroup in the offspring of blood group O parents.
  Transfus Med, 15, 435-442.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.