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- PDB-6uyr: Crystal structure of K46-acetylated SUMO1 in complex with PML-SIM -

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Basic information

Entry
Database: PDB / ID: 6uyr
TitleCrystal structure of K46-acetylated SUMO1 in complex with PML-SIM
Components
  • Protein PML
  • Small ubiquitin-related modifier 1
KeywordsNUCLEAR PROTEIN/PROTEIN BINDING / SUMO1 / PML / SUMO INTERACTION MOTIF / PHOSPHOSIM / NUCLEAR PROTEIN-PROTEIN BINDING complex
Function / homology
Function and homology information


regulation of calcium ion transport into cytosol / ubiquitin-like protein ligase activity / negative regulation of translation in response to oxidative stress / positive regulation of protein localization to chromosome, telomeric region / positive regulation of peptidyl-lysine acetylation / suppression of viral release by host / protein localization to nuclear pore / negative regulation of transcription by transcription factor localization / SUMOylation of nuclear envelope proteins / Negative regulation of activity of TFAP2 (AP-2) family transcription factors ...regulation of calcium ion transport into cytosol / ubiquitin-like protein ligase activity / negative regulation of translation in response to oxidative stress / positive regulation of protein localization to chromosome, telomeric region / positive regulation of peptidyl-lysine acetylation / suppression of viral release by host / protein localization to nuclear pore / negative regulation of transcription by transcription factor localization / SUMOylation of nuclear envelope proteins / Negative regulation of activity of TFAP2 (AP-2) family transcription factors / SUMO is proteolytically processed / negative regulation of delayed rectifier potassium channel activity / SUMO is conjugated to E1 (UBA2:SAE1) / PML body organization / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / nuclear stress granule / negative regulation of action potential / small protein activating enzyme binding / SUMO binding / positive regulation of apoptotic process involved in mammary gland involution / : / fibroblast migration / SMAD protein signal transduction / positive regulation of telomere maintenance / regulation of calcium ion transmembrane transport / regulation of double-strand break repair / myeloid cell differentiation / SUMOylation of DNA methylation proteins / SUMOylation of immune response proteins / maintenance of protein location in nucleus / XY body / SUMOylation of SUMOylation proteins / protein-containing complex localization / Maturation of nucleoprotein / endoplasmic reticulum calcium ion homeostasis / Transferases; Acyltransferases; Aminoacyltransferases / regulation of cardiac muscle cell contraction / positive regulation of extrinsic apoptotic signaling pathway / SUMOylation of RNA binding proteins / oncogene-induced cell senescence / Regulation of RUNX1 Expression and Activity / branching involved in mammary gland duct morphogenesis / SUMO transferase activity / Postmitotic nuclear pore complex (NPC) reformation / Maturation of nucleoprotein / negative regulation of interleukin-1 beta production / intrinsic apoptotic signaling pathway in response to oxidative stress / cobalt ion binding / negative regulation of protein import into nucleus / roof of mouth development / SUMOylation of ubiquitinylation proteins / transcription factor binding / ubiquitin-specific protease binding / entrainment of circadian clock by photoperiod / negative regulation of DNA binding / SMAD binding / ubiquitin-like protein ligase binding / negative regulation of telomere maintenance via telomerase / positive regulation of signal transduction by p53 class mediator / SUMOylation of transcription factors / SUMOylation of DNA replication proteins / protein sumoylation / negative regulation of mitotic cell cycle / intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress / intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / cell fate commitment / protein targeting / regulation of cell adhesion / cellular response to interleukin-4 / potassium channel regulator activity / retinoic acid receptor signaling pathway / negative regulation of ubiquitin-dependent protein catabolic process / nuclear pore / Regulation of IFNG signaling / SUMOylation of DNA damage response and repair proteins / response to UV / positive regulation of defense response to virus by host / extrinsic apoptotic signaling pathway / Regulation of TP53 Activity through Acetylation / DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest / cellular response to cadmium ion / negative regulation of angiogenesis / SUMOylation of chromatin organization proteins / Regulation of PTEN localization / transforming growth factor beta receptor signaling pathway / SUMOylation of transcription cofactors / cellular response to leukemia inhibitory factor / response to cytokine / response to gamma radiation / circadian regulation of gene expression / SUMOylation of intracellular receptors / positive regulation of protein-containing complex assembly / negative regulation of DNA-binding transcription factor activity / PKR-mediated signaling / negative regulation of cell growth / regulation of circadian rhythm / PML body / nuclear matrix / Formation of Incision Complex in GG-NER / HCMV Early Events
Similarity search - Function
Protein of unknown function DUF3583 / PML-like, coiled-coil / : / ANCHR-like B-box zinc-binding domain / Small ubiquitin-related modifier 1, Ubl domain / Rad60/SUMO-like domain / Ubiquitin-2 like Rad60 SUMO-like / B-Box-type zinc finger / B-box-type zinc finger / Zinc finger B-box type profile. ...Protein of unknown function DUF3583 / PML-like, coiled-coil / : / ANCHR-like B-box zinc-binding domain / Small ubiquitin-related modifier 1, Ubl domain / Rad60/SUMO-like domain / Ubiquitin-2 like Rad60 SUMO-like / B-Box-type zinc finger / B-box-type zinc finger / Zinc finger B-box type profile. / Zinc finger, C3HC4 RING-type / Zinc finger, C3HC4 type (RING finger) / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Ring finger / Zinc finger RING-type profile. / Zinc finger, RING-type / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Zinc finger, RING/FYVE/PHD-type / Ubiquitin-like domain superfamily
Similarity search - Domain/homology
Protein PML / Small ubiquitin-related modifier 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.3 Å
AuthorsWahba, H.M. / Gagnon, C. / Mascle, X.H. / Lussier-Price, M. / Cappadocia, L. / Sakaguchi, K. / Omichinski, J.G.
Funding support Canada, 2items
OrganizationGrant numberCountry
Canadian Institutes of Health Research (CIHR)74739 Canada
Canadian Institutes of Health Research (CIHR)130414 Canada
CitationJournal: Structure / Year: 2020
Title: Acetylation of SUMO1 Alters Interactions with the SIMs of PML and Daxx in a Protein-Specific Manner.
Authors: Mascle, X.H. / Gagnon, C. / Wahba, H.M. / Lussier-Price, M. / Cappadocia, L. / Sakaguchi, K. / Omichinski, J.G.
History
DepositionNov 14, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 27, 2019Provider: repository / Type: Initial release
Revision 1.1Jan 8, 2020Group: Author supporting evidence / Database references / Category: citation / citation_author / pdbx_audit_support
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID / _pdbx_audit_support.funding_organization
Revision 1.2Feb 19, 2020Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.year
Revision 1.3Oct 11, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 2.0Nov 15, 2023Group: Atomic model / Data collection / Category: atom_site / chem_comp_atom / chem_comp_bond
Item: _atom_site.auth_atom_id / _atom_site.label_atom_id ..._atom_site.auth_atom_id / _atom_site.label_atom_id / _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2
Revision 2.1Oct 30, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Small ubiquitin-related modifier 1
B: Protein PML


Theoretical massNumber of molelcules
Total (without water)12,5452
Polymers12,5452
Non-polymers00
Water2,270126
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: isothermal titration calorimetry
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)38.373, 47.070, 63.179
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein Small ubiquitin-related modifier 1 / SUMO-1 / GAP-modifying protein 1 / GMP1 / SMT3 homolog 3 / Sentrin / Ubiquitin-homology domain ...SUMO-1 / GAP-modifying protein 1 / GMP1 / SMT3 homolog 3 / Sentrin / Ubiquitin-homology domain protein PIC1 / Ubiquitin-like protein SMT3C / Smt3C / Ubiquitin-like protein UBL1


Mass: 9567.801 Da / Num. of mol.: 1 / Mutation: C52A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SUMO1, SMT3C, SMT3H3, UBL1, OK/SW-cl.43 / Plasmid: PGEX2T / Production host: Escherichia coli (E. coli) / References: UniProt: P63165
#2: Protein/peptide Protein PML / Promyelocytic leukemia protein / RING finger protein 71 / Tripartite motif-containing protein 19


Mass: 2976.985 Da / Num. of mol.: 1 / Mutation: E574Y
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PML, MYL, PP8675, RNF71, TRIM19 / Plasmid: PGEX2T / Production host: Escherichia coli (E. coli) / References: UniProt: P29590
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 126 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.27 Å3/Da / Density % sol: 45.91 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop
Details: 100MM SODIUM CACODYLATE PH6.5, 16% PEG3350, 10MM CALCIUM CHLORIDE

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: CLSI / Beamline: 08ID-1 / Wavelength: 0.9795 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Jul 29, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 1.3→32.797 Å / Num. obs: 28366 / % possible obs: 98.36 % / Redundancy: 6 % / CC1/2: 0.999 / Net I/σ(I): 16.26
Reflection shellResolution: 1.3→1.347 Å / Num. unique obs: 2449 / CC1/2: 0.392 / % possible all: 85.27

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Processing

Software
NameVersionClassification
PHENIX1.14-3260_1496refinement
PDB_EXTRACT3.25data extraction
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4WJO

4wjo


Resolution: 1.3→32.797 Å / SU ML: 0.15 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 17.15
RfactorNum. reflection% reflection
Rfree0.1733 2000 7.05 %
Rwork0.1561 --
obs0.1574 28360 98.36 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 58.62 Å2 / Biso mean: 20.6163 Å2 / Biso min: 10.78 Å2
Refinement stepCycle: final / Resolution: 1.3→32.797 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms746 0 0 126 872
Biso mean---33.1 -
Num. residues----91
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
1.3005-1.3330.33251150.3163150980
1.333-1.3690.27771410.255186898
1.369-1.40930.26781420.22111875100
1.4093-1.45480.23341420.18131860100
1.4548-1.50680.19531420.15021883100
1.5068-1.56710.20791450.13671889100
1.5671-1.63840.17181430.12491896100
1.6384-1.72480.16131430.12981888100
1.7248-1.83290.16231450.12631915100
1.8329-1.97440.15771450.12941905100
1.9744-2.1730.14591460.13021923100
2.173-2.48740.17371470.14481932100
2.4874-3.13340.17821480.16131961100
3.1334-32.7970.15791560.17122056100

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