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PDBsum entry 5kni
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PDB id:
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Transferase
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Title:
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Crystal structure of the wild-type sam domain of human tankyrase-1
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Structure:
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Tankyrase-1. Chain: a, b, c, d, e, f, g. Fragment: unp residues 1026 to 1092. Synonym: tank1,adp-ribosyltransferase diphtheria toxin-like 5,artd5, poly [adp-ribose] polymerase 5a,tnks-1,trf1-interacting ankyrin- related adp-ribose polymerase,tankyrase i. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: tnks, parp5a, parpl, tin1, tinf1, tnks1. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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2.50Å
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R-factor:
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0.170
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R-free:
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0.212
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Authors:
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J.M.Pascal,M.Mccauley,M.F.Langelier,A.A.Riccio
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Key ref:
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A.A.Riccio
et al.
(2016).
Tankyrase Sterile α Motif Domain Polymerization Is Required for Its Role in Wnt Signaling.
Structure,
24,
1573-1581.
PubMed id:
DOI:
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Date:
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28-Jun-16
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Release date:
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31-Aug-16
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PROCHECK
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Headers
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References
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O95271
(TNKS1_HUMAN) -
Poly [ADP-ribose] polymerase tankyrase-1 from Homo sapiens
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Seq:
Struc:
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1327 a.a.
58 a.a.
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Enzyme class 1:
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Chains A, B, C, D, E, F, G:
E.C.2.4.2.-
- ?????
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Enzyme class 2:
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Chains A, B, C, D, E, F, G:
E.C.2.4.2.30
- NAD(+) ADP-ribosyltransferase.
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Pathway:
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Reaction:
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NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D- ribosyl)n+1-acceptor + H+
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NAD(+)
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+
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(ADP-D-ribosyl)n-acceptor
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=
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nicotinamide
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+
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(ADP-D- ribosyl)n+1-acceptor
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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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DOI no:
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Structure
24:1573-1581
(2016)
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PubMed id:
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Tankyrase Sterile α Motif Domain Polymerization Is Required for Its Role in Wnt Signaling.
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A.A.Riccio,
M.McCauley,
M.F.Langelier,
J.M.Pascal.
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ABSTRACT
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Tankyrase-1 (TNKS1/PARP-5a) is a poly(ADP-ribose) polymerase (PARP) enzyme that
regulates multiple cellular processes creating a poly(ADP-ribose)
posttranslational modification that can lead to target protein turnover. TNKS1
thereby controls protein levels of key components of signaling pathways,
including Axin1, the limiting component of the destruction complex in canonical
Wnt signaling that degrades β-catenin to prevent its coactivator function in
gene expression. There are limited molecular level insights into TNKS1
regulation in cell signaling pathways. TNKS1 has a sterile α motif (SAM) domain
that is known to mediate polymerization, but the functional requirement for SAM
polymerization has not been assessed. We have determined the crystal structure
of wild-type human TNKS1 SAM domain and used structure-based mutagenesis to
disrupt polymer formation and assess the consequences on TNKS1 regulation of
β-catenin-dependent transcription. Our data indicate the SAM polymer is
critical for TNKS1 catalytic activity and allows TNKS1 to efficiently access
cytoplasmic signaling complexes.
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