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- PDB-1v66: Solution structure of human p53 binding domain of PIAS-1 -

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Basic information

Entry
Database: PDB / ID: 1v66
TitleSolution structure of human p53 binding domain of PIAS-1
ComponentsProtein inhibitor of activated STAT protein 1
KeywordsLIGASE / four helix bundle / RIKEN Structural Genomics/Proteomics Initiative / RSGI / Structural Genomics
Function / homology
Function and homology information


RNA polymerase II-specific DNA-binding transcription factor binding => GO:0061629 / regulation of type II interferon-mediated signaling pathway / protein-DNA complex assembly / SUMO ligase activity / positive regulation of smooth muscle cell differentiation / : / positive regulation of protein sumoylation / Transferases; Acyltransferases; Aminoacyltransferases / SUMO transferase activity / SUMOylation of ubiquitinylation proteins ...RNA polymerase II-specific DNA-binding transcription factor binding => GO:0061629 / regulation of type II interferon-mediated signaling pathway / protein-DNA complex assembly / SUMO ligase activity / positive regulation of smooth muscle cell differentiation / : / positive regulation of protein sumoylation / Transferases; Acyltransferases; Aminoacyltransferases / SUMO transferase activity / SUMOylation of ubiquitinylation proteins / fat cell differentiation / cell surface receptor signaling pathway via JAK-STAT / SUMOylation of transcription factors / protein sumoylation / SUMOylation of DNA damage response and repair proteins / Regulation of IFNG signaling / SUMOylation of chromatin organization proteins / SUMOylation of transcription cofactors / transcription coregulator activity / SUMOylation of intracellular receptors / visual learning / PML body / Formation of Incision Complex in GG-NER / G1/S transition of mitotic cell cycle / transcription corepressor activity / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / regulation of cell population proliferation / spermatogenesis / nuclear speck / protein domain specific binding / ubiquitin protein ligase binding / regulation of transcription by RNA polymerase II / negative regulation of apoptotic process / positive regulation of DNA-templated transcription / enzyme binding / negative regulation of transcription by RNA polymerase II / DNA binding / zinc ion binding / nucleoplasm / nucleus
Similarity search - Function
PINIT domain / PINIT domain superfamily / PINIT domain / PINIT domain profile. / MIZ/SP-RING zinc finger / SAP domain / Zinc finger, MIZ-type / Zinc finger SP-RING-type profile. / Transcription Termination Factor Rho, Rna-binding Domain; Chain A, Domain 1 / SAP domain superfamily ...PINIT domain / PINIT domain superfamily / PINIT domain / PINIT domain profile. / MIZ/SP-RING zinc finger / SAP domain / Zinc finger, MIZ-type / Zinc finger SP-RING-type profile. / Transcription Termination Factor Rho, Rna-binding Domain; Chain A, Domain 1 / SAP domain superfamily / SAP motif profile. / Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation / SAP domain / Zinc finger, RING/FYVE/PHD-type / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
E3 SUMO-protein ligase PIAS1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR
AuthorsOkubo, S. / Hara, F. / Tsuchida, Y. / Shimotakahara, S. / Suzuki, S. / Hatanaka, H. / Yokoyama, S. / Tanaka, H. / Yasuda, H. / Shindo, H. / RIKEN Structural Genomics/Proteomics Initiative (RSGI)
CitationJournal: J.Biol.Chem. / Year: 2004
Title: NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA oligomers
Authors: Okubo, S. / Hara, F. / Tsuchida, Y. / Shimotakahara, S. / Suzuki, S. / Hatanaka, H. / Yokoyama, S. / Tanaka, H. / Yasuda, H. / Shindo, H.
History
DepositionNov 27, 2003Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Dec 7, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.4Dec 27, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Protein inhibitor of activated STAT protein 1


Theoretical massNumber of molelcules
Total (without water)7,4671
Polymers7,4671
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / -
Representative

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Components

#1: Protein Protein inhibitor of activated STAT protein 1 / protein inhibitor of activated STAT-1 / PIAS-1 / Gu binding protein / GBP / RNA helicase II binding ...protein inhibitor of activated STAT-1 / PIAS-1 / Gu binding protein / GBP / RNA helicase II binding protein / DEAD/H box-binding protein 1


Mass: 7466.976 Da / Num. of mol.: 1 / Fragment: residues 1-65
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: pET28b / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: O75925

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1

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Processing

NMR softwareName: CYANA / Developer: Guentert, P. / Classification: refinement
NMR ensembleConformers submitted total number: 20

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