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PDBsum entry 1zi3

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protein ligands metals links
Transferase PDB id
1zi3
Jmol
Contents
Protein chain
263 a.a. *
Ligands
NLC
Metals
_HG ×4
_CL
Waters ×200
* Residue conservation analysis
PDB id:
1zi3
Name: Transferase
Title: Crystal structure of human n-acetylgalactosaminyltransferase complexed with n-acetyllactosamine
Structure: Histo-blood group abo system transferase (nagat) glycoprotein-fucosylgalactoside alpha-n- acetylgalactosaminyltransferase. Chain: a. Synonym: fucosylglycoprotein alpha-n-acetylgalactosaminyltr (histo-blood group a transferase) (a transferase). Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: abo. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
Resolution:
1.69Å     R-factor:   0.209     R-free:   0.234
Authors: J.A.Letts,N.L.Rose,Y.R.Fang,C.H.Barry,S.N.Borisova,N.O.Seto, M.M.Palcic,S.V.Evans
Key ref:
J.A.Letts et al. (2006). Differential Recognition of the Type I and II H Antigen Acceptors by the Human ABO(H) Blood Group A and B Glycosyltransferases. J Biol Chem, 281, 3625-3632. PubMed id: 16326711 DOI: 10.1074/jbc.M507620200
Date:
26-Apr-05     Release date:   13-Dec-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P16442  (BGAT_HUMAN) -  Histo-blood group ABO system transferase
Seq:
Struc:
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.2.4.1.37  - 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
UDP-alpha-D-galactose
+
alpha-L-fucosyl-(1->2)-D-galactosyl-R
Bound ligand (Het Group name = NLC)
matches with 63.33% similarity
= UDP
+ alpha-D-galactosyl-(1->3)-(alpha-L-fucosyl-(1->2))-D-galactosyl-R
   Enzyme class 2: E.C.2.4.1.40  - 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
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
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  

 

 
    reference    
 
 
DOI no: 10.1074/jbc.M507620200 J Biol Chem 281:3625-3632 (2006)
PubMed id: 16326711  
 
 
Differential Recognition of the Type I and II H Antigen Acceptors by the Human ABO(H) Blood Group A and B Glycosyltransferases.
J.A.Letts, N.L.Rose, Y.R.Fang, C.H.Barry, S.N.Borisova, N.O.Seto, M.M.Palcic, S.V.Evans.
 
  ABSTRACT  
 
The human ABO(H) blood group A and B antigens are generated by the homologous glycosyltransferases A (GTA) and B (GTB), which add the monosaccharides GalNAc and Gal, respectively, to the cell-surface H antigens. In the first comprehensive structural study of the recognition by a glycosyltransferase of a panel of substrates corresponding to acceptor fragments, 14 high resolution crystal structures of GTA and GTB have been determined in the presence of oligosaccharides corresponding to different segments of the type I (alpha-l-Fucp-(1-->2)-beta-d-Galp-(1-->3)-beta-d-GlcNAcp-OR, where R is a glycoprotein or glycolipid in natural acceptors) and type II (alpha-l-Fucp-(1-->2)-beta-d-Galp-(1-->4)-beta-d-GlcNAcp-OR) H antigen trisaccharides. GTA and GTB differ in only four "critical" amino acid residues (Arg/Gly-176, Gly/Ser-235, Leu/Met-266, and Gly/Ala-268). As these enzymes both utilize the H antigen acceptors, the four critical residues had been thought to be involved strictly in donor recognition; however, we now report that acceptor binding and subsequent transfer are significantly influenced by two of these residues: Gly/Ser-235 and Leu/Met-266. Furthermore, these structures show that acceptor recognition is dominated by the central Gal residue despite the fact that the l-Fuc residue is required for efficient catalysis and give direct insight into the design of model inhibitors for GTA and GTB.
 
  Selected figure(s)  
 
Figure 3.
Environment surrounding the Gal monosaccharide in GTA (left) and GTB (right) showing how the critical residues affect acceptor recognition. Atoms in the protein are colored red for oxygen, white for carbon, and blue for nitrogen. Water molecules are shown as cyan spheres. Hydrogen bonds are shown by green dotted lines. Acceptor fragments are shown in yellow.
Figure 4.
Environment surrounding the disaccharide acceptor fragment analogs Lac, ╬▓MeLac, and LacNAc (a, b, and d) in GTB and LacNAc in GTA (c) showing how the critical residues affect acceptor recognition. Atoms in the protein are colored red for oxygen, white for carbon, and blue for nitrogen. Water molecules are shown as cyan spheres. Hydrogen bonds are shown by green dotted lines. Acceptor fragments are shown in yellow.
 
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2006, 281, 3625-3632) copyright 2006.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21098513 N.Soya, Y.Fang, M.M.Palcic, and J.S.Klassen (2011).
Trapping and characterization of covalent intermediates of mutant retaining glycosyltransferases.
  Glycobiology, 21, 547-552.  
20154292 N.Sindhuwinata, E.Munoz, F.J.Munoz, M.M.Palcic, H.Peters, and T.Peters (2010).
Binding of an acceptor substrate analog enhances the enzymatic activity of human blood group B galactosyltransferase.
  Glycobiology, 20, 718-723.  
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.  
17392366 S.Cao, Z.Lou, M.Tan, Y.Chen, Y.Liu, Z.Zhang, X.C.Zhang, X.Jiang, X.Li, and Z.Rao (2007).
Structural basis for the recognition of blood group trisaccharides by norovirus.
  J Virol, 81, 5949-5957.
PDB codes: 2obr 2obs 2obt
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.