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PDBsum entry 5a01
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PDB id:
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Transferase
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Title:
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O-glcnac transferase from drososphila melanogaster
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Structure:
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O-glycosyltransferase. Chain: a, b, c. Fragment: catalytic domain and 4.5 tpr, unp residues 352-1059. Synonym: o-glcnac transferase. Engineered: yes. Mutation: yes
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Source:
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Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_variant: ril.
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Resolution:
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2.66Å
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R-factor:
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0.227
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R-free:
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0.264
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Authors:
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D.Mariappa,X.Zheng,M.Schimpl,O.Raimi,K.Rafie,A.T.Ferenbach, H.J.Mueller,D.M.F.Van Aalten
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Key ref:
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D.Mariappa
et al.
(2015).
Dual functionality of O-GlcNAc transferase is required for Drosophila development.
Open Biol,
5,
150234.
PubMed id:
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Date:
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15-Apr-15
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Release date:
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27-Apr-16
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PROCHECK
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Headers
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References
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Q7KJA9
(Q7KJA9_DROME) -
protein O-GlcNAc transferase from Drosophila melanogaster
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Seq:
Struc:
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1059 a.a.
681 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 3 residue positions (black
crosses)
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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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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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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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Open Biol
5:150234
(2015)
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PubMed id:
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Dual functionality of O-GlcNAc transferase is required for Drosophila development.
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D.Mariappa,
X.Zheng,
M.Schimpl,
O.Raimi,
A.T.Ferenbach,
H.A.Müller,
D.M.van Aalten.
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ABSTRACT
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Post-translational modification of intracellular proteins with O-linked
N-acetylglucosamine (O-GlcNAc) catalysed by O-GlcNAc transferase (OGT) has been
linked to regulation of diverse cellular functions. OGT possesses a C-terminal
glycosyltransferase catalytic domain and N-terminal tetratricopeptide repeats
that are implicated in protein-protein interactions. Drosophila OGT (DmOGT) is
encoded by super sex combs (sxc), mutants of which are pupal lethal. However, it
is not clear if this phenotype is caused by reduction of O-GlcNAcylation. Here
we use a genetic approach to demonstrate that post-pupal Drosophila development
can proceed with negligible OGT catalysis, while early embryonic development is
OGT activity-dependent. Structural and enzymatic comparison between human OGT
(hOGT) and DmOGT informed the rational design of DmOGT point mutants with a
range of reduced catalytic activities. Strikingly, a severely hypomorphic OGT
mutant complements sxc pupal lethality. However, the hypomorphic OGT
mutant-rescued progeny do not produce F2 adults, because a set of Hox genes is
de-repressed in F2 embryos, resulting in homeotic phenotypes. Thus, OGT
catalytic activity is required up to late pupal stages, while further
development proceeds with severely reduced OGT activity.
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Links
