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PDBsum entry 1fr8

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protein ligands Protein-protein interface(s) links
Transferase PDB id
1fr8
Jmol
Contents
Protein chains
271 a.a. *
Ligands
GDU ×2
Waters ×79
* Residue conservation analysis
PDB id:
1fr8
Name: Transferase
Title: Crystal structure of the bovine beta 1,4 galactosyltransferase (b4galt1) catalytic domain complexed with uridine diphosphogalactose
Structure: Beta 1,4 galactosyltransferase. Chain: a, b. Fragment: catalytic domain. Synonym: beta4galt1. Engineered: yes
Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: liver. Expressed in: mus musculus. Expression_system_taxid: 10090. Expression_system_cell_line: nso.
Biol. unit: Tetramer (from PQS)
Resolution:
2.40Å     R-factor:   0.237     R-free:   0.262
Authors: L.N.Gastinel,C.Cambillau,Y.Bourne
Key ref:
L.N.Gastinel et al. (1999). Crystal structures of the bovine beta4galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose. EMBO J, 18, 3546-3557. PubMed id: 10393171 DOI: 10.1093/emboj/18.13.3546
Date:
07-Sep-00     Release date:   20-Sep-00    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P08037  (B4GT1_BOVIN) -  Beta-1,4-galactosyltransferase 1
Seq:
Struc:
402 a.a.
271 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 1: E.C.2.4.1.22  - Lactose synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: UDP-alpha-D-galactose + D-glucose = UDP + lactose
UDP-alpha-D-galactose
+ D-glucose
=
UDP
Bound ligand (Het Group name = GDU)
corresponds exactly
+ lactose
   Enzyme class 2: E.C.2.4.1.38  - Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: UDP-alpha-D-galactose + N-acetyl-beta-D-glucosaminylglycopeptide = UDP + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminylglycopeptide
UDP-alpha-D-galactose
+ N-acetyl-beta-D-glucosaminylglycopeptide
=
UDP
Bound ligand (Het Group name = GDU)
corresponds exactly
+ beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminylglycopeptide
   Enzyme class 3: E.C.2.4.1.90  - N-acetyllactosamine synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine
UDP-alpha-D-galactose
+ N-acetyl-D-glucosamine
=
UDP
Bound ligand (Het Group name = GDU)
corresponds exactly
+ N-acetyllactosamine
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!
  Biological process     carbohydrate metabolic process   1 term 
  Biochemical function     transferase activity, transferring glycosyl groups     1 term  

 

 
    reference    
 
 
DOI no: 10.1093/emboj/18.13.3546 EMBO J 18:3546-3557 (1999)
PubMed id: 10393171  
 
 
Crystal structures of the bovine beta4galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose.
L.N.Gastinel, C.Cambillau, Y.Bourne.
 
  ABSTRACT  
 
beta1,4-galactosyltransferase T1 (beta4Gal-T1, EC 2.4.1.90/38), a Golgi resident membrane-bound enzyme, transfers galactose from uridine diphosphogalactose to the terminal beta-N-acetylglucosamine residues forming the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids. In mammals, beta4Gal-T1 binds to alpha-lactalbumin, a protein that is structurally homologous to lyzozyme, to produce lactose. beta4Gal-T1 is a member of a large family of homologous beta4galactosyltransferases that use different types of glycoproteins and glycolipids as substrates. Here we solved and refined the crystal structures of recombinant bovine beta4Gal-T1 to 2.4 A resolution in the presence and absence of the substrate uridine diphosphogalactose. The crystal structure of the bovine substrate-free beta4Gal-T1 catalytic domain showed a new fold consisting of a single conical domain with a large open pocket at its base. In the substrate-bound complex, the pocket encompassed residues interacting with uridine diphosphogalactose. The structure of the complex contained clear regions of electron density for the uridine diphosphate portion of the substrate, where its beta-phosphate group was stabilized by hydrogen-bonding contacts with conserved residues including the Asp252ValAsp254 motif. These results help the interpretation of engineered beta4Gal-T1 point mutations. They suggest a mechanism possibly involved in galactose transfer and enable identification of the critical amino acids involved in alpha-lactalbumin interactions.
 
  Selected figure(s)  
 
Figure 2.
Figure 2 (A) Close-up stereoview of the 4Gal-T1 substrate binding site. The UDP portion of UDP-Gal is coloured yellow in ball-and-stick, where a water molecule is given as a grey sphere. Amino acid side-chains interacting with UDP are indicated by red sticks and labelled. (B) Stereoview of the electron density omit map (2 ) of the UDP-Gal binding site. (C) LIGPLOT diagram of 4Gal-T1 amino acids interacting with the UDP portion of UDP-Gal. Ligand bonds are in purple, non-ligand bonds are in light brown, hydrogen bonds are green dashed lines. Ligand atoms are surrounded by a yellow circle if highly accessible and a brown circle if buried. Non-ligand residues in hydrophobic contacts with the ligand are presented by red semi-circles with radiating spokes.
Figure 5.
Figure 5 Close-up stereo view of the superimposition of UMP from the substrate-free structure and UDP from the substrate-bound complex structure. (A) UMP and UDP are given in ball-and-stick forms where pink stands for UMP and red for UDP-Gal. 4Gal-T1 structure from the 4Gal-T1 structure complexed with UDP-Gal is shown as a ribbon diagram with amino acid side-chains interacting with UMP or UDP-Gal shown in a ball-and-stick form in yellow. (B) LIGPLOT representation of 4Gal-T1 amino acids interacting with UMP. The LIGPLOT legend is the same as in Figure 2C.
 
  The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (1999, 18, 3546-3557) copyright 1999.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20625591 K.Lau, V.Thon, H.Yu, L.Ding, Y.Chen, M.M.Muthana, D.Wong, R.Huang, and X.Chen (2010).
Highly efficient chemoenzymatic synthesis of beta1-4-linked galactosides with promiscuous bacterial beta1-4-galactosyltransferases.
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20364127 T.Pesnot, R.Jørgensen, M.M.Palcic, and G.K.Wagner (2010).
Structural and mechanistic basis for a new mode of glycosyltransferase inhibition.
  Nat Chem Biol, 6, 321-323.
PDB codes: 3ioh 3ioi 3ioj
18712827 A.D.Schuyler, R.L.Jernigan, P.K.Qasba, B.Ramakrishnan, and G.S.Chirikjian (2009).
Iterative cluster-NMA: A tool for generating conformational transitions in proteins.
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18673333 E.A.Landers, H.R.Burkin, G.T.Bleck, L.Howell-Skalla, and D.J.Miller (2009).
Porcine beta1,4-galactosyltransferase-I sequence and expression.
  Reprod Domest Anim, 44, 228-234.  
19106107 J.R.Brown, F.Yang, A.Sinha, B.Ramakrishnan, Y.Tor, P.K.Qasba, and J.D.Esko (2009).
Deoxygenated Disaccharide Analogs as Specific Inhibitors of {beta}1-4-Galactosyltransferase 1 and Selectin-mediated Tumor Metastasis.
  J Biol Chem, 284, 4952-4959.
PDB code: 3ee5
19028689 K.B.Luther, H.Schindelin, and R.S.Haltiwanger (2009).
Structural and mechanistic insights into lunatic fringe from a kinetic analysis of enzyme mutants.
  J Biol Chem, 284, 3294-3305.  
19003527 S.I.Do (2009).
Generation of novel chimeric LacdiNAcS by gene fusion of alpha-lactalbumin and beta1,4-galactosyltransferase 1.
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18627619 C.J.Zea, G.Camci-Unal, and N.L.Pohl (2008).
Thermodynamics of binding of divalent magnesium and manganese to uridine phosphates: implications for diabetes-related hypomagnesaemia and carbohydrate biocatalysis.
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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.  
18393823 P.K.Qasba, B.Ramakrishnan, and E.Boeggeman (2008).
Structure and function of beta -1,4-galactosyltransferase.
  Curr Drug Targets, 9, 292-309.  
17850816 A.L.Milac, N.V.Buchete, T.A.Fritz, G.Hummer, and L.A.Tabak (2007).
Substrate-induced conformational changes and dynamics of UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase-2.
  J Mol Biol, 373, 439-451.  
17151241 N.Haines, and B.A.Stewart (2007).
Functional roles for beta1,4-N-acetlygalactosaminyltransferase-A in Drosophila larval neurons and muscles.
  Genetics, 175, 671-679.  
16840342 E.T.Larson, D.Reiter, M.Young, and C.M.Lawrence (2006).
Structure of A197 from Sulfolobus turreted icosahedral virus: a crenarchaeal viral glycosyltransferase exhibiting the GT-A fold.
  J Virol, 80, 7636-7644.
PDB code: 2c0n
17032646 K.Kozma, J.J.Keusch, B.Hegemann, K.B.Luther, D.Klein, D.Hess, R.S.Haltiwanger, and J.Hofsteenge (2006).
Identification and characterization of abeta1,3-glucosyltransferase that synthesizes the Glc-beta1,3-Fuc disaccharide on thrombospondin type 1 repeats.
  J Biol Chem, 281, 36742-36751.  
16847057 M.E.Deadman, S.L.Lundström, E.K.Schweda, E.R.Moxon, and D.W.Hood (2006).
Specific amino acids of the glycosyltransferase LpsA direct the addition of glucose or galactose to the terminal inner core heptose of Haemophilus influenzae lipopolysaccharide via alternative linkages.
  J Biol Chem, 281, 29455-29467.  
16815917 M.Fondeur-Gelinotte, V.Lattard, R.Oriol, R.Mollicone, J.C.Jacquinet, G.Mulliert, S.Gulberti, P.Netter, J.Magdalou, M.Ouzzine, and S.Fournel-Gigleux (2006).
Phylogenetic and mutational analyses reveal key residues for UDP-glucuronic acid binding and activity of beta1,3-glucuronosyltransferase I (GlcAT-I).
  Protein Sci, 15, 1667-1678.  
16512410 Y.Sadakane, and Y.Hatanaka (2006).
Photochemical fishing approaches for identifying target proteins and elucidating the structure of a ligand-binding region using carbene-generating photoreactive probes.
  Anal Sci, 22, 209-218.  
16007668 C.J.Zea, and N.L.Pohl (2005).
Unusual sugar nucleotide recognition elements of mesophilic vs. thermophilic glycogen synthases.
  Biopolymers, 79, 106-113.  
15485809 L.Yin (2005).
Chondroitin synthase 1 is a key molecule in myeloma cell-osteoclast interactions.
  J Biol Chem, 280, 15666-15672.  
15987364 M.H.Yazer, G.A.Denomme, N.L.Rose, and M.M.Palcic (2005).
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  Transfusion, 45, 1178-1182.  
15653326 P.K.Qasba, B.Ramakrishnan, and E.Boeggeman (2005).
Substrate-induced conformational changes in glycosyltransferases.
  Trends Biochem Sci, 30, 53-62.  
15849187 T.D.Hurley, S.Stout, E.Miner, J.Zhou, and P.J.Roach (2005).
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  J Biol Chem, 280, 23892-23899.
PDB codes: 1zct 1zcu 1zcv 1zcy 1zdf 1zdg
15465321 B.Ramakrishnan, E.Boeggeman, V.Ramasamy, and P.K.Qasba (2004).
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15067013 K.Angata, D.Chan, J.Thibault, and M.Fukuda (2004).
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14760744 K.Gunasekaran, and R.Nussinov (2004).
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  Chembiochem, 5, 224-230.  
15148316 M.L.Rosén, M.Edman, M.Sjöström, and A.Wieslander (2004).
Recognition of fold and sugar linkage for glycosyltransferases by multivariate sequence analysis.
  J Biol Chem, 279, 38683-38692.  
14752117 Y.D.Lobsanov, P.A.Romero, B.Sleno, B.Yu, P.Yip, A.Herscovics, and P.L.Howell (2004).
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PDB codes: 1s4n 1s4o 1s4p
14646108 C.Horcajada, E.Cid, J.J.Guinovart, N.Verdaguer, and J.C.Ferrer (2003).
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  Acta Crystallogr D Biol Crystallogr, 59, 2322-2324.  
12590131 H.Takemae, R.Ueda, R.Okubo, H.Nakato, S.Izumi, K.Saigo, and S.Nishihara (2003).
Proteoglycan UDP-galactose:beta-xylose beta 1,4-galactosyltransferase I is essential for viability in Drosophila melanogaster.
  J Biol Chem, 278, 15571-15578.  
12743367 T.Correia, V.Papayannopoulos, V.Panin, P.Woronoff, J.Jiang, T.F.Vogt, and K.D.Irvine (2003).
Molecular genetic analysis of the glycosyltransferase Fringe in Drosophila.
  Proc Natl Acad Sci U S A, 100, 6404-6409.  
12803927 T.D.Butters, H.R.Mellor, K.Narita, R.A.Dwek, and F.M.Platt (2003).
Small-molecule therapeutics for the treatment of glycolipid lysosomal storage disorders.
  Philos Trans R Soc Lond B Biol Sci, 358, 927-945.  
12966086 T.Sato, M.Gotoh, K.Kiyohara, A.Kameyama, T.Kubota, N.Kikuchi, Y.Ishizuka, H.Iwasaki, A.Togayachi, T.Kudo, T.Ohkura, H.Nakanishi, and H.Narimatsu (2003).
Molecular cloning and characterization of a novel human beta 1,4-N-acetylgalactosaminyltransferase, beta 4GalNAc-T3, responsible for the synthesis of N,N'-diacetyllactosediamine, galNAc beta 1-4GlcNAc.
  J Biol Chem, 278, 47534-47544.  
12954635 T.Y.Yen, B.A.Macher, S.Bryson, X.Chang, I.Tvaroska, R.Tse, S.Takeshita, A.M.Lew, and A.Datti (2003).
Highly conserved cysteines of mouse core 2 beta1,6-N-acetylglucosaminyltransferase I form a network of disulfide bonds and include a thiol that affects enzyme activity.
  J Biol Chem, 278, 45864-45881.  
12538870 Y.Hu, L.Chen, S.Ha, B.Gross, B.Falcone, D.Walker, M.Mokhtarzadeh, and S.Walker (2003).
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  Proc Natl Acad Sci U S A, 100, 845-849.
PDB code: 1nlm
12011052 E.Boix, Y.Zhang, G.J.Swaminathan, K.Brew, and K.R.Acharya (2002).
Structural basis of ordered binding of donor and acceptor substrates to the retaining glycosyltransferase, alpha-1,3-galactosyltransferase.
  J Biol Chem, 277, 28310-28318.
PDB codes: 1gwv 1gww 1gx0 1gx4
11784313 H.Ihara, Y.Ikeda, S.Koyota, T.Endo, K.Honke, and N.Taniguchi (2002).
A catalytically inactive beta 1,4-N-acetylglucosaminyltransferase III (GnT-III) behaves as a dominant negative GnT-III inhibitor.
  Eur J Biochem, 269, 193-201.  
12235155 J.Stolz, and S.Munro (2002).
The components of the Saccharomyces cerevisiae mannosyltransferase complex M-Pol I have distinct functions in mannan synthesis.
  J Biol Chem, 277, 44801-44808.  
11950836 L.C.Pedersen, T.A.Darden, and M.Negishi (2002).
Crystal structure of beta 1,3-glucuronyltransferase I in complex with active donor substrate UDP-GlcUA.
  J Biol Chem, 277, 21869-21873.
PDB code: 1kws
12163485 M.Gotoh, T.Sato, T.Akashima, H.Iwasaki, A.Kameyama, H.Mochizuki, T.Yada, N.Inaba, Y.Zhang, N.Kikuchi, Y.D.Kwon, A.Togayachi, T.Kudo, S.Nishihara, H.Watanabe, K.Kimata, and H.Narimatsu (2002).
Enzymatic synthesis of chondroitin with a novel chondroitin sulfate N-acetylgalactosaminyltransferase that transfers N-acetylgalactosamine to glucuronic acid in initiation and elongation of chondroitin sulfate synthesis.
  J Biol Chem, 277, 38189-38196.  
11784317 M.Malissard, A.Dinter, E.G.Berger, and T.Hennet (2002).
Functional assignment of motifs conserved in beta 1,3-glycosyltransferases.
  Eur J Biochem, 269, 233-239.  
12199709 M.Tenno, S.Toba, F.J.Kézdy, A.P.Elhammer, and A.Kurosaka (2002).
Identification of two cysteine residues involved in the binding of UDP-GalNAc to UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1).
  Eur J Biochem, 269, 4308-4316.  
11943783 P.E.Pummill, and P.L.DeAngelis (2002).
Evaluation of critical structural elements of UDP-sugar substrates and certain cysteine residues of a vertebrate hyaluronan synthase.
  J Biol Chem, 277, 21610-21616.  
11807274 R.P.Gibson, R.M.Lloyd, S.J.Charnock, and G.J.Davies (2002).
Characterization of Escherichia coli OtsA, a trehalose-6-phosphate synthase from glycosyltransferase family 20.
  Acta Crystallogr D Biol Crystallogr, 58, 349-351.  
12198488 S.I.Patenaude, N.O.Seto, S.N.Borisova, A.Szpacenko, S.L.Marcus, M.M.Palcic, and S.V.Evans (2002).
The structural basis for specificity in human ABO(H) blood group biosynthesis.
  Nat Struct Biol, 9, 685-690.
PDB codes: 1lz0 1lz7 1lzi 1lzj
11821425 T.Iwai, N.Inaba, A.Naundorf, Y.Zhang, M.Gotoh, H.Iwasaki, T.Kudo, A.Togayachi, Y.Ishizuka, H.Nakanishi, and H.Narimatsu (2002).
Molecular cloning and characterization of a novel UDP-GlcNAc:GalNAc-peptide beta1,3-N-acetylglucosaminyltransferase (beta 3Gn-T6), an enzyme synthesizing the core 3 structure of O-glycans.
  J Biol Chem, 277, 12802-12809.  
12215432 Y.Nakamura, N.Haines, J.Chen, T.Okajima, K.Furukawa, T.Urano, P.Stanley, K.D.Irvine, and K.Furukawa (2002).
Identification of a Drosophila gene encoding xylosylprotein beta4-galactosyltransferase that is essential for the synthesis of glycosaminoglycans and for morphogenesis.
  J Biol Chem, 277, 46280-46288.  
12167666 Z.S.Kawar, I.Van Die, and R.D.Cummings (2002).
Molecular cloning and enzymatic characterization of a UDP-GalNAc:GlcNAc(beta)-R beta1,4-N-acetylgalactosaminyltransferase from Caenorhabditis elegans.
  J Biol Chem, 277, 34924-34932.  
11731297 C.Saotome, C.H.Wong, and O.Kanie (2001).
Combinatorial library of five-membered iminocyclitol and the inhibitory activities against glyco-enzymes.
  Chem Biol, 8, 1061-1070.  
11573090 D.A.Sanders, A.G.Staines, S.A.McMahon, M.R.McNeil, C.Whitfield, and J.H.Naismith (2001).
UDP-galactopyranose mutase has a novel structure and mechanism.
  Nat Struct Biol, 8, 858-863.
PDB code: 1i8t
11410375 D.Hoffmeister, K.Ichinose, and A.Bechthold (2001).
Two sequence elements of glycosyltransferases involved in urdamycin biosynthesis are responsible for substrate specificity and enzymatic activity.
  Chem Biol, 8, 557-567.  
  11592969 E.Boix, G.J.Swaminathan, Y.Zhang, R.Natesh, K.Brew, and K.R.Acharya (2001).
Structure of UDP complex of UDP-galactose:beta-galactoside-alpha -1,3-galactosyltransferase at 1.53-A resolution reveals a conformational change in the catalytically important C terminus.
  J Biol Chem, 276, 48608-48614.
PDB code: 1k4v
11398978 E.J.Hehre (2001).
Glycosyl transfer: a history of the concept's development and view of its major contributions to biochemistry.
  Carbohydr Res, 331, 347-368.  
11746818 I.Gromova, P.Gromov, and J.E.Celis (2001).
A novel member of the glycosyltransferase family, beta 3 Gn-T2, highly downregulated in invasive human bladder transitional cell carcinomas.
  Mol Carcinog, 32, 61-72.  
11179209 L.N.Gastinel, C.Bignon, A.K.Misra, O.Hindsgaul, J.H.Shaper, and D.H.Joziasse (2001).
Bovine alpha1,3-galactosyltransferase catalytic domain structure and its relationship with ABO histo-blood group and glycosphingolipid glycosyltransferases.
  EMBO J, 20, 638-649.
PDB codes: 1fg5 1g8o 1g93
11488931 M.Malissard, and E.G.Berger (2001).
Improving solubility of catalytic domain of human beta-1,4-galactosyltransferase 1 through rationally designed amino acid replacements.
  Eur J Biochem, 268, 4352-4358.  
11484220 M.Rao, and I.Tvaroska (2001).
Structure of bovine alpha-1,3-galactosyltransferase and its complexes with UDP and DPGal inferred from molecular modeling.
  Proteins, 44, 428-434.  
11285558 P.Petrová, C.Monteiro, C.Hervé du Penhoat, J.Koca, and A.Imberty (2001).
Conformational behavior of nucleotide-sugar in solution: molecular dynamics and NMR study of solvated uridine diphosphate-glucose in the presence of monovalent cations.
  Biopolymers, 58, 617-635.  
11717264 V.Chazalet, K.Uehara, R.A.Geremia, and C.Breton (2001).
Identification of essential amino acids in the Azorhizobium caulinodans fucosyltransferase NodZ.
  J Bacteriol, 183, 7067-7075.  
11114903 W.J.Keenleyside, A.J.Clarke, and C.Whitfield (2001).
Identification of residues involved in catalytic activity of the inverting glycosyl transferase WbbE from Salmonella enterica serovar borreze.
  J Bacteriol, 183, 77-85.  
11785761 Y.Bourne, and B.Henrissat (2001).
Glycoside hydrolases and glycosyltransferases: families and functional modules.
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11212123 Y.Hatanaka, M.Ishiguro, M.Hashimoto, L.N.Gastinel, and K.Nakagomi (2001).
A model of photoprobe docking with beta1,4-galactosyltransferase identifies a possible carboxylate involved in glycosylation steps.
  Bioorg Med Chem Lett, 11, 411-413.  
11226175 Y.Maeda, R.Watanabe, C.L.Harris, Y.Hong, K.Ohishi, K.Kinoshita, and T.Kinoshita (2001).
PIG-M transfers the first mannose to glycosylphosphatidylinositol on the lumenal side of the ER.
  EMBO J, 20, 250-261.  
10788427 C.Busch, F.Hofmann, R.Gerhard, and K.Aktories (2000).
Involvement of a conserved tryptophan residue in the UDP-glucose binding of large clostridial cytotoxin glycosyltransferases.
  J Biol Chem, 275, 13228-13234.  
11042449 C.Busch, and K.Aktories (2000).
Microbial toxins and the glycosylation of rho family GTPases.
  Curr Opin Struct Biol, 10, 528-535.  
11035748 C.Busch, K.Schömig, F.Hofmann, and K.Aktories (2000).
Characterization of the catalytic domain of Clostridium novyi alpha-toxin.
  Infect Immun, 68, 6378-6383.  
11074385 I.M.Saxena, and R.M.Brown (2000).
Cellulose synthases and related enzymes.
  Curr Opin Plant Biol, 3, 523-531.  
10935637 K.Brückner, L.Perez, H.Clausen, and S.Cohen (2000).
Glycosyltransferase activity of Fringe modulates Notch-Delta interactions.
  Nature, 406, 411-415.  
  10892798 S.Ha, D.Walker, Y.Shi, and S.Walker (2000).
The 1.9 A crystal structure of Escherichia coli MurG, a membrane-associated glycosyltransferase involved in peptidoglycan biosynthesis.
  Protein Sci, 9, 1045-1052.
PDB code: 1f0k
10899003 S.Munro, and M.Freeman (2000).
The notch signalling regulator fringe acts in the Golgi apparatus and requires the glycosyltransferase signature motif DXD.
  Curr Biol, 10, 813-820.  
10972999 T.Y.Yen, R.K.Joshi, H.Yan, N.O.Seto, M.M.Palcic, and B.A.Macher (2000).
Characterization of cysteine residues and disulfide bonds in proteins by liquid chromatography/electrospray ionization tandem mass spectrometry.
  J Mass Spectrom, 35, 990.  
11042447 U.M.Unligil, and J.M.Rini (2000).
Glycosyltransferase structure and mechanism.
  Curr Opin Struct Biol, 10, 510-517.  
11032794 U.M.Unligil, S.Zhou, S.Yuwaraj, M.Sarkar, H.Schachter, and J.M.Rini (2000).
X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily.
  EMBO J, 19, 5269-5280.
PDB codes: 1fo8 1fo9 1foa
10608830 B.Lougheed, H.D.Ly, W.W.Wakarchuk, and S.G.Withers (1999).
Glycosyl fluorides can function as substrates for nucleotide phosphosugar-dependent glycosyltransferases.
  J Biol Chem, 274, 37717-37722.  
10508766 C.Breton, and A.Imberty (1999).
Structure/function studies of glycosyltransferases.
  Curr Opin Struct Biol, 9, 563-571.  
10600700 M.M.Palcic (1999).
Biocatalytic synthesis of oligosaccharides.
  Curr Opin Biotechnol, 10, 616-624.  
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