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PDBsum entry 5c8r
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PDB id:
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Transferase
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Title:
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Crystal structure of abba + udp-glc + di
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Structure:
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Histo-blood group abo system transferase. Chain: a. Fragment: unp residues 64-354. Synonym: fucosylglycoprotein 3-alpha-galactosyltransferase, fucosylglycoprotein alpha-n-acetylgalactosaminyltransferase, glycoprotein-fucosylgalactoside alpha-n- acetylgalactosaminyltransferase,glycoprotein-fucosylgalactoside alpha-galactosyltransferase,histo-blood group a transferase,a transferase,histo-blood group b transferase,b transferase,nagat.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: abo. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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1.45Å
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R-factor:
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0.176
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R-free:
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0.186
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Authors:
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S.Gagnon,P.Meloncelli,R.B.Zheng,O.Haji-Ghassemi,A.R.Johal,S.Borisova, T.L.Lowary,S.V.Evans
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Key ref:
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S.M.Gagnon
et al.
(2015).
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.
J Biol Chem,
290,
27040-27052.
PubMed id:
DOI:
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Date:
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26-Jun-15
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Release date:
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23-Sep-15
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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.
278 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 6 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(+)
Bound ligand (Het Group name = )
matches with 69.44% similarity
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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(+)
Bound ligand (Het Group name = )
matches with 69.44% similarity
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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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DOI no:
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J Biol Chem
290:27040-27052
(2015)
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PubMed id:
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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.
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S.M.Gagnon,
P.J.Meloncelli,
R.B.Zheng,
O.Haji-Ghassemi,
A.R.Johal,
S.N.Borisova,
T.L.Lowary,
S.V.Evans.
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ABSTRACT
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Homologous glycosyltransferases α-(1→3)-N-acetylgalactosaminyltransferase
(GTA) and α-(1→3)-galactosyltransferase (GTB) catalyze the final step in
ABO(H) blood group A and B antigen synthesis through sugar transfer from
activated donor to the H antigen acceptor. These enzymes have a GT-A fold type
with characteristic mobile polypeptide loops that cover the active site upon
substrate binding and, despite intense investigation, many aspects of substrate
specificity and catalysis remain unclear. The structures of GTA, GTB, and their
chimeras have been determined to between 1.55 and 1.39 Å resolution in complex
with natural donors UDP-Gal, UDP-Glc and, in an attempt to overcome one of the
common problems associated with three-dimensional studies, the non-hydrolyzable
donor analog UDP-phosphono-galactose (UDP-C-Gal). Whereas the uracil moieties of
the donors are observed to maintain a constant location, the sugar moieties lie
in four distinct conformations, varying from extended to the "tucked
under" conformation associated with catalysis, each stabilized by different
hydrogen bonding partners with the enzyme. Further, several structures show
clear evidence that the donor sugar is disordered over two of the observed
conformations and so provide evidence for stepwise insertion into the active
site. Although the natural donors can both assume the tucked under conformation
in complex with enzyme, UDP-C-Gal cannot. Whereas UDP-C-Gal was designed to be
"isosteric" with natural donor, the small differences in structure
imposed by changing the epimeric oxygen atom to carbon appear to render the
enzyme incapable of binding the analog in the active conformation and so
preclude its use as a substrate mimic in GTA and GTB.
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