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PDBsum entry 4xi9
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PDB id:
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Transferase
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Title:
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Human ogt in complex with udp-5s-glcnac and substrate peptide (rbl2)
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Structure:
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Udp-n-acetylglucosamine--peptide n- acetylglucosaminyltransferase 110 kda subunit. Chain: a, b, c, d. Fragment: unp residues 323-1041. Synonym: o-glcnac transferase subunit p110,o-linked n- acetylglucosamine transferase 110 kda subunit,ogt. Engineered: yes. Retinoblastoma-like protein 2. Chain: e, f, g, h.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: ogt. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 9606
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Resolution:
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3.10Å
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R-factor:
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0.203
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R-free:
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0.223
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Authors:
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M.Schimpl,D.M.F.Van Aalten
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Key ref:
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S.Pathak
et al.
(2015).
The active site of O-GlcNAc transferase imposes constraints on substrate sequence.
Nat Struct Biol,
22,
744-750.
PubMed id:
DOI:
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Date:
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06-Jan-15
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Release date:
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05-Aug-15
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PROCHECK
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Headers
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References
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O15294
(OGT1_HUMAN) -
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit from Homo sapiens
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Seq:
Struc:
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1046 a.a.
698 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 1 residue position (black
cross)
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Enzyme class:
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E.C.2.4.1.255
- protein O-GlcNAc transferase.
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Reaction:
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1.
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L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl- beta-D-glucosaminyl)-L-seryl-[protein] + UDP + H+
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2.
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L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O- (N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + UDP + H+
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L-seryl-[protein]
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+
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UDP-N-acetyl-alpha-D-glucosamine
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=
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3-O-(N-acetyl- beta-D-glucosaminyl)-L-seryl-[protein]
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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 64.10% similarity
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L-threonyl-[protein]
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+
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UDP-N-acetyl-alpha-D-glucosamine
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=
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3-O- (N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein]
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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 64.10% similarity
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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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Nat Struct Biol
22:744-750
(2015)
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PubMed id:
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The active site of O-GlcNAc transferase imposes constraints on substrate sequence.
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S.Pathak,
J.Alonso,
M.Schimpl,
K.Rafie,
D.E.Blair,
V.S.Borodkin,
A.W.Schüttelkopf,
O.Albarbarawi,
D.M.van Aalten.
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ABSTRACT
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O-GlcNAc transferase (OGT) glycosylates a diverse range of intracellular
proteins with O-linked N-acetylglucosamine (O-GlcNAc), an essential and dynamic
post-translational modification in metazoans. Although this enzyme modifies
hundreds of proteins with O-GlcNAc, it is not understood how OGT achieves
substrate specificity. In this study, we describe the application of a
high-throughput OGT assay to a library of peptides. We mapped sites of O-GlcNAc
modification by electron transfer dissociation MS and found that they correlate
with previously detected O-GlcNAc sites. Crystal structures of four acceptor
peptides in complex with Homo sapiens OGT suggest that a combination of size and
conformational restriction defines sequence specificity in the -3 to +2
subsites. This work reveals that although the N-terminal TPR repeats of OGT may
have roles in substrate recognition, the sequence restriction imposed by the
peptide-binding site makes a substantial contribution to O-GlcNAc site
specificity.
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Links
