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- PDB-5zba: Crystal structure of Rtt109-Asf1-H3-H4-CoA complex -

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Basic information

Entry
Database: PDB / ID: 5zba
TitleCrystal structure of Rtt109-Asf1-H3-H4-CoA complex
Components
  • DNA damage response protein Rtt109, putative
  • Histone H3
  • Histone H4
  • Histone chaperone asf1
KeywordsTRANSFERASE/STRUCTURAL PROTEIN / Histone / acetylation / chaperone / DNA replication / nucleosome assembly / DNA damage / TRANSFERASE / TRANSFERASE-STRUCTURAL PROTEIN complex
Function / homology
Function and homology information


histone H3K56 acetyltransferase activity / H3 histone acetyltransferase complex / DNA replication-dependent chromatin disassembly / sexual sporulation resulting in formation of a cellular spore / HDMs demethylate histones / HATs acetylate histones / Condensation of Prophase Chromosomes / global genome nucleotide-excision repair / RNA polymerase I upstream activating factor complex / acetyltransferase activator activity ...histone H3K56 acetyltransferase activity / H3 histone acetyltransferase complex / DNA replication-dependent chromatin disassembly / sexual sporulation resulting in formation of a cellular spore / HDMs demethylate histones / HATs acetylate histones / Condensation of Prophase Chromosomes / global genome nucleotide-excision repair / RNA polymerase I upstream activating factor complex / acetyltransferase activator activity / DNA replication-dependent chromatin assembly / SUMOylation of chromatin organization proteins / nucleosome disassembly / : / replication fork protection complex / RMTs methylate histone arginines / silent mating-type cassette heterochromatin formation / positive regulation of transcription by RNA polymerase I / nucleolar large rRNA transcription by RNA polymerase I / subtelomeric heterochromatin formation / rRNA transcription / CENP-A containing nucleosome / histone acetyltransferase / positive regulation of transcription elongation by RNA polymerase II / regulation of protein phosphorylation / nucleosome assembly / structural constituent of chromatin / nucleosome / chromatin organization / histone binding / chromosome, telomeric region / protein heterodimerization activity / DNA damage response / regulation of DNA-templated transcription / DNA binding / nucleus / cytosol
Similarity search - Function
Histone acetyltransferase Rtt109 / Rtt109-type histone acetyltransferase (HAT) domain profile. / Histone deposition protein Asf1 / Histone chaperone ASF1-like / Histone chaperone ASF1-like / Histone chaperone ASF1-like superfamily / ASF1 like histone chaperone / Histone acetyltransferase Rtt109/CBP / Histone acetylation protein / Histone acetylation protein ...Histone acetyltransferase Rtt109 / Rtt109-type histone acetyltransferase (HAT) domain profile. / Histone deposition protein Asf1 / Histone chaperone ASF1-like / Histone chaperone ASF1-like / Histone chaperone ASF1-like superfamily / ASF1 like histone chaperone / Histone acetyltransferase Rtt109/CBP / Histone acetylation protein / Histone acetylation protein / Histone, subunit A / Histone, subunit A / Histone H4, conserved site / Histone H4 signature. / Histone H4 / Histone H4 / CENP-T/Histone H4, histone fold / Centromere kinetochore component CENP-T histone fold / Histone H3 signature 1. / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 / Histone-fold / Immunoglobulin-like / Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
COENZYME A / IODIDE ION / Histone H4 / Histone H3 / histone acetyltransferase / Histone chaperone asf1
Similarity search - Component
Biological speciesNeosartorya fumigata (mold)
Saccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3.5 Å
AuthorsZhang, L. / Serra-Cardona, A. / Zhou, H. / Wang, M. / Yang, N. / Zhang, Z. / Xu, R.M.
Funding support China, United States, 7items
OrganizationGrant numberCountry
NSFC31210103914 China
NSFC31521002 China
NSFC31430018 China
Ministry of Science and Technology of China2015CB856200 China
Chinese Academy of SciencesXDB08010100 China
Beijing Municipal Science and Technology ProjectZ171100000417001 China
NIHGM118015 United States
CitationJournal: Cell / Year: 2018
Title: Multisite Substrate Recognition in Asf1-Dependent Acetylation of Histone H3 K56 by Rtt109.
Authors: Zhang, L. / Serra-Cardona, A. / Zhou, H. / Wang, M. / Yang, N. / Zhang, Z. / Xu, R.M.
History
DepositionFeb 10, 2018Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jul 25, 2018Provider: repository / Type: Initial release
Revision 1.1Aug 22, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_abbrev / _citation.journal_id_CSD ..._citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Nov 22, 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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: DNA damage response protein Rtt109, putative
B: Histone chaperone asf1
C: Histone H3
D: Histone H4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)113,03242
Polymers107,5694
Non-polymers5,46338
Water0
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area19050 Å2
ΔGint-64 kcal/mol
Surface area29380 Å2
MethodPISA
Unit cell
Length a, b, c (Å)111.903, 111.903, 332.715
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number179
Space group name H-MP6522
Components on special symmetry positions
IDModelComponents
11C-204-

IOD

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Components

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Protein , 4 types, 4 molecules ABCD

#1: Protein DNA damage response protein Rtt109, putative


Mass: 59684.863 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (mold)
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100 / Gene: AFUA_5G09540 / Plasmid: pET28a-smt3 / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: Q4WUS9
#2: Protein Histone chaperone asf1 / Anti-silencing function protein 1


Mass: 21097.975 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (mold)
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100 / Gene: asf1, AFUA_3G11030 / Plasmid: pET28a / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: Q4WXX5
#3: Protein Histone H3 /


Mass: 15391.007 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c / Gene: HHT1, YBR010W, YBR0201, HHT2, SIN2, YNL031C, N2749 / Plasmid: pETDuet / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P61830
#4: Protein Histone H4 /


Mass: 11395.390 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c / Gene: HHF1, YBR009C, YBR0122, HHF2, YNL030W, N2752 / Plasmid: pETDuet / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P02309

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Non-polymers , 2 types, 38 molecules

#5: Chemical ChemComp-COA / COENZYME A / Coenzyme A


Mass: 767.534 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C21H36N7O16P3S
#6: Chemical...
ChemComp-IOD / IODIDE ION / Iodide


Mass: 126.904 Da / Num. of mol.: 37 / Source method: obtained synthetically / Formula: I

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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: 2.8 Å3/Da / Density % sol: 56 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 5
Details: 100mM sodium citrate, pH 5.0, 22% PEG 1500, 400mM sodium iodide

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 0.9785 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 3, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9785 Å / Relative weight: 1
ReflectionResolution: 3.5→50 Å / Num. obs: 16416 / % possible obs: 99.5 % / Redundancy: 5.2 % / Biso Wilson estimate: 68.52 Å2 / Rmerge(I) obs: 0.177 / Rpim(I) all: 0.08 / Rrim(I) all: 0.196 / Χ2: 1.147 / Net I/σ(I): 4.3 / Num. measured all: 85255
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
3.5-3.635.40.52715870.7770.240.5851.15199.7
3.63-3.775.50.41615730.8760.1850.461.12299.4
3.77-3.945.50.34415970.8910.1540.381.13299.7
3.94-4.155.30.23916150.9650.1080.2651.20199.8
4.15-4.415.20.18416110.970.0830.2041.14699.9
4.41-4.7550.13916210.9790.0650.1551.13499.6
4.75-5.235.50.1316310.9860.0570.1431.13699.5
5.23-5.985.30.15116480.9790.0680.1671.1799.5
5.98-7.534.80.11216930.9890.0530.1261.14699.4
7.53-504.70.05818400.9980.0280.0651.13598.9

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
PDB_EXTRACT3.24data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5ZB9, 2HUE

5zb9

2hue


Resolution: 3.5→42.825 Å / SU ML: 0.47 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 26.75 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2945 828 5.08 %
Rwork0.2429 15458 -
obs0.2454 16286 99.43 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 129.19 Å2 / Biso mean: 65.8467 Å2 / Biso min: 42.99 Å2
Refinement stepCycle: final / Resolution: 3.5→42.825 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5449 0 85 0 5534
Biso mean--68.84 --
Num. residues----688
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0035623
X-RAY DIFFRACTIONf_angle_d0.4977640
X-RAY DIFFRACTIONf_chiral_restr0.02862
X-RAY DIFFRACTIONf_plane_restr0.003978
X-RAY DIFFRACTIONf_dihedral_angle_d10.2062067
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 6

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.5001-3.71930.33921440.304424902634100
3.7193-4.00630.33951400.276225032643100
4.0063-4.40910.33191390.259425332672100
4.4091-5.04620.27311510.22492528267999
5.0462-6.35440.31271390.2492598273799
6.3544-42.8280.21841150.19952806292199

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