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- PDB-1y0j: Zinc fingers as protein recognition motifs: structural basis for ... -

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Basic information

Entry
Database: PDB / ID: 1y0j
TitleZinc fingers as protein recognition motifs: structural basis for the GATA-1/Friend of GATA interaction
Components
  • Erythroid transcription factor
  • Zinc-finger protein ush
KeywordsDNA BINDING PROTEIN / zinc finger / GATA-1 / FOG / protein-protein complex
Function / homology
Function and homology information


lymph gland plasmatocyte differentiation / lymph gland crystal cell differentiation / negative regulation of hemocyte differentiation / amnioserosa maintenance / positive regulation of antibacterial peptide biosynthetic process / regulation of primitive erythrocyte differentiation / basophil differentiation / eosinophil fate commitment / regulation of definitive erythrocyte differentiation / germ-band shortening ...lymph gland plasmatocyte differentiation / lymph gland crystal cell differentiation / negative regulation of hemocyte differentiation / amnioserosa maintenance / positive regulation of antibacterial peptide biosynthetic process / regulation of primitive erythrocyte differentiation / basophil differentiation / eosinophil fate commitment / regulation of definitive erythrocyte differentiation / germ-band shortening / larval lymph gland hemopoiesis / lymph gland development / Factors involved in megakaryocyte development and platelet production / compound eye development / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / regulation of glycoprotein biosynthetic process / megakaryocyte differentiation / chaeta development / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / cell development / RUNX1 regulates transcription of genes involved in differentiation of HSCs / Sertoli cell development / dendritic cell differentiation / Factors involved in megakaryocyte development and platelet production / positive regulation of mast cell degranulation / cellular response to follicle-stimulating hormone stimulus / negative regulation of bone mineralization / myeloid cell differentiation / C2H2 zinc finger domain binding / embryonic hemopoiesis / platelet formation / DNA binding, bending / DNA-binding transcription repressor activity / positive regulation of osteoblast proliferation / animal organ regeneration / negative regulation of extrinsic apoptotic signaling pathway in absence of ligand / cell fate commitment / cis-regulatory region sequence-specific DNA binding / erythrocyte development / transcription repressor complex / negative regulation of insulin receptor signaling pathway / positive regulation of erythrocyte differentiation / homeostasis of number of cells within a tissue / cellular response to cAMP / transcription coregulator binding / erythrocyte differentiation / RNA polymerase II transcription regulatory region sequence-specific DNA binding / protein-DNA complex / chromatin DNA binding / platelet aggregation / male gonad development / transcription coactivator binding / sequence-specific double-stranded DNA binding / p53 binding / cell-cell signaling / heart development / cellular response to lipopolysaccharide / positive regulation of cytosolic calcium ion concentration / DNA-binding transcription activator activity, RNA polymerase II-specific / transcription regulator complex / sequence-specific DNA binding / in utero embryonic development / RNA polymerase II-specific DNA-binding transcription factor binding / DNA-binding transcription factor activity, RNA polymerase II-specific / cell differentiation / transcription cis-regulatory region binding / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / negative regulation of cell population proliferation / negative regulation of DNA-templated transcription / chromatin binding / regulation of DNA-templated transcription / negative regulation of apoptotic process / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / DNA binding / zinc ion binding / nucleoplasm / nucleus
Similarity search - Function
: / Zinc finger protein 462, seventh C2H2 zinc finger / Zinc finger CCHC FOG-type / FOG family / Zinc finger CCHC FOG-type profile. / Transcription factor GATA / GATA-type zinc finger domain. / GATA-type zinc finger domain profile. / zinc finger binding to DNA consensus sequence [AT]GATA[AG] / GATA zinc finger ...: / Zinc finger protein 462, seventh C2H2 zinc finger / Zinc finger CCHC FOG-type / FOG family / Zinc finger CCHC FOG-type profile. / Transcription factor GATA / GATA-type zinc finger domain. / GATA-type zinc finger domain profile. / zinc finger binding to DNA consensus sequence [AT]GATA[AG] / GATA zinc finger / Zinc finger, GATA-type / Zinc-finger of C2H2 type / zinc finger / Zinc finger C2H2 type domain profile. / Zinc finger C2H2 superfamily / Zinc finger C2H2-type / Zinc finger, NHR/GATA-type
Similarity search - Domain/homology
Erythroid transcription factor / Zinc finger protein ush
Similarity search - Component
Biological speciesMus musculus (house mouse)
Drosophila melanogaster (fruit fly)
MethodSOLUTION NMR / simulated annealing, molecular dynamics torsion angle dynamics
AuthorsLiew, C.K. / Simpson, R.J.Y. / Kwan, A.H.Y. / Crofts, L.A. / Loughlin, F.E. / Matthews, J.M. / Crossley, M. / Mackay, J.P.
CitationJournal: Proc.Natl.Acad.Sci.Usa / Year: 2005
Title: Zinc fingers as protein recognition motifs: Structural basis for the GATA-1/Friend of GATA interaction
Authors: Liew, C.K. / Simpson, R.J.Y. / Kwan, A.H.Y. / Crofts, L.A. / Loughlin, F.E. / Matthews, J.M. / Crossley, M. / Mackay, J.P.
History
DepositionNov 15, 2004Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Jan 25, 2005Provider: repository / Type: Initial release
Revision 1.1Oct 16, 2007Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4May 29, 2024Group: 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: Erythroid transcription factor
B: Zinc-finger protein ush
hetero molecules


Theoretical massNumber of molelcules
Total (without water)9,2924
Polymers9,1622
Non-polymers1312
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 / 100structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein/peptide Erythroid transcription factor / GATA-1 / Eryf1 / GF-1 / NF-E1


Mass: 5199.939 Da / Num. of mol.: 1 / Fragment: GNF
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: gata-1 / Plasmid: pGEX-2T / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P17679
#2: Protein/peptide Zinc-finger protein ush / U-SHAPED TRANSCRIPTION FACTOR / U-shaped protein


Mass: 3961.636 Da / Num. of mol.: 1 / Fragment: USF1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Drosophila melanogaster (fruit fly) / Gene: u-shaped / Plasmid: pGEX-2T / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q9VPQ6
#3: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111HNCO
121HNCA
133HNCA
143HN(CO)CA
152HNCA
162CBCA(CO)NH
17215N, 13C double decoupled NOESY
182(H)CCH-TOCSY
19415N, 13C double half-filtered NOESY
1104HN(CA)CB
NMR detailsText: Other commonly used standard triple-resonance NMR experiments were also recorded.

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Sample preparation

Details
Solution-IDContentsSolvent system
10.5mM GNF U-15N,13C; 2mM tris-carboxyethylphosphine (TCEP); 1mM zinc sulphate; 20mM Sodium Acetate95% H2O/5% D2O
20.5mM GNF U-15N,13C; 0.6mM USF1; 2mM tris-carboxyethylphosphine (TCEP); 1mM zinc sulphate; 20mM Sodium Acetate95% H2O/5% D2O
30.5mM USF1 U-15N,13C; 2mM tris-carboxyethylphosphine (TCEP); 1mM zinc sulphate; 20mM Sodium Acetate95% H2O/5% D2O
40.5mM GNF; 0.6mM USF1 U-15N,13C; 2mM tris-carboxyethylphosphine (TCEP); 1mM zinc sulphate; 20mM Sodium Acetate95% H2O/5% D2O
Sample conditionspH: 5.5 / Pressure: ambient / Temperature: 280 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
XwinNMR2.5Brukerprocessing
XEASY1.3.13Bartels et aldata analysis
ARIA1.2Linge et alstructure solution
HADDOCK1Donminguez et alstructure solution
HADDOCK1Donminguez et alrefinement
RefinementMethod: simulated annealing, molecular dynamics torsion angle dynamics
Software ordinal: 1
Details: Standard triple-resonance NMR spectroscopy was first used to determine the preliminary structure of the complex. Since the backbone folds of both GNF and USF1 did not appear to be ...Details: Standard triple-resonance NMR spectroscopy was first used to determine the preliminary structure of the complex. Since the backbone folds of both GNF and USF1 did not appear to be substantially altered to those of the proteins in isolation, the computer program Haddock was used to dock the two partner proteins using intermolecular NOEs obtained from double half-filtered NOESY experiments, and ambiguous restraints derived from mutagenesis and NMR titration experiments.
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 20

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