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PDBsum entry 3ioh
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Contents |
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* Residue conservation analysis
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PDB id:
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Transferase
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Title:
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Crystal structure of the fucosylgalactoside alpha n- acetylgalactosaminyltransferase (gta, cisab mutant l266g, g268a)
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Structure:
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Histo-blood group abo system transferase. Chain: a. Fragment: extracellular catalytic domain. Synonym: nagat, glycoprotein-fucosylgalactoside alpha-n- acetylgalactosaminyltransferase, fucosylglycoprotein alpha-n- acetylgalactosaminyltransferase, histo-blood group a transferase, a transferase, glycoprotein-fucosylgalactoside alpha- galactosyltransferase, fucosylglycoprotein 3-alpha- galactosyltransferase, histo-blood group b transferase, b
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: abo. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
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Resolution:
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1.25Å
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R-factor:
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0.153
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R-free:
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0.177
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Authors:
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T.Pesnot,R.Jorgensen,M.M.Palcic,G.K.Wagner
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Key ref:
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T.Pesnot
et al.
(2010).
Structural and mechanistic basis for a new mode of glycosyltransferase inhibition.
Nat Chem Biol,
6,
321-323.
PubMed id:
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Date:
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14-Aug-09
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Release date:
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07-Apr-10
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PROCHECK
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Headers
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References
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P16442
(BGAT_HUMAN) -
Histo-blood group ABO system transferase from Homo sapiens
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Seq:
Struc:
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354 a.a.
283 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 3 residue positions (black
crosses)
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Enzyme class 1:
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E.C.2.4.1.37
- fucosylgalactoside 3-alpha-galactosyltransferase.
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Reaction:
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an alpha-L-fucosyl-(1->2)-beta-D-galactosyl derivative + UDP-alpha-D- galactose = an alpha-D-galactosyl-(1->3)-[alpha-L-fucosyl-(1->2)]-beta-D- galactosyl derivative + UDP + H+
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alpha-L-fucosyl-(1->2)-beta-D-galactosyl derivative
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+
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UDP-alpha-D- galactose
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=
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alpha-D-galactosyl-(1->3)-[alpha-L-fucosyl-(1->2)]-beta-D- galactosyl derivative
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+
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UDP
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+
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H(+)
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Enzyme class 2:
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E.C.2.4.1.40
- glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase.
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Reaction:
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an alpha-L-fucosyl-(1->2)-beta-D-galactosyl derivative + UDP-N-acetyl- alpha-D-galactosamine = an N-acetyl-alpha-D-galactosaminyl-(1->3)-[alpha- L-fucosyl-(1->2)]-beta-D-galactosyl derivative + UDP + H+
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alpha-L-fucosyl-(1->2)-beta-D-galactosyl derivative
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+
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UDP-N-acetyl- alpha-D-galactosamine
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=
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N-acetyl-alpha-D-galactosaminyl-(1->3)-[alpha- L-fucosyl-(1->2)]-beta-D-galactosyl derivative
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+
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UDP
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+
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H(+)
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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.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Nat Chem Biol
6:321-323
(2010)
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PubMed id:
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Structural and mechanistic basis for a new mode of glycosyltransferase inhibition.
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T.Pesnot,
R.Jørgensen,
M.M.Palcic,
G.K.Wagner.
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ABSTRACT
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Glycosyltransferases are carbohydrate-active enzymes with essential roles in
numerous important biological processes. We have developed a new donor analog
for galactosyltransferases that locks a representative target enzyme in a
catalytically inactive conformation, thus almost completely abolishing sugar
transfer. Results with other galactosyltransferases suggest that this unique
mode of glycosyltransferase inhibition may also be generally applicable to other
members of this important enzyme family.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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K.Descroix,
and
G.K.Wagner
(2011).
The first C-glycosidic analogue of a novel galactosyltransferase inhibitor.
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Org Biomol Chem,
9,
1855-1863.
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N.Soya,
Y.Fang,
M.M.Palcic,
and
J.S.Klassen
(2011).
Trapping and characterization of covalent intermediates of mutant retaining glycosyltransferases.
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Glycobiology,
21,
547-552.
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T.M.Gloster,
W.F.Zandberg,
J.E.Heinonen,
D.L.Shen,
L.Deng,
and
D.J.Vocadlo
(2011).
Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells.
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Nat Chem Biol,
7,
174-181.
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Z.L.Wu,
C.M.Ethen,
B.Prather,
M.Machacek,
and
W.Jiang
(2011).
Universal phosphatase-coupled glycosyltransferase assay.
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Glycobiology,
21,
727-733.
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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.
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Links
