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- SASDFK7: Complex with 1H histone chaperone Asf1, histones H3 (35-135aa) an... -

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Basic information

Entry
Database: SASBDB / ID: SASDFK7
SampleComplex with 1H histone chaperone Asf1, histones H3 (35-135aa) and H4; 70%-2H histone acetyltransferase Rtt109 and histone chaperone Vps75 (1-225aa) acquired in 100% v/v D2O
  • Vacuolar protein sorting-associated protein 75 (1-225 aa) (protein), Vps75 1-225, Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
  • Histone acetyltransferase RTT109 (protein), Rtt109, Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
  • Histone chaperone ASF1 (protein), Asf1
  • Histone H3.2 (35-135 aa) (protein), H3 (35-135), Xenopus laevis
  • Histone H4 (protein), H4, Xenopus laevis
Function / homology
Function and homology information


Formation of Senescence-Associated Heterochromatin Foci (SAHF) / H3 histone acetyltransferase complex / regulation of double-strand break repair via nonhomologous end joining / maintenance of rDNA / replication-born double-strand break repair via sister chromatid exchange / transposable element silencing / histone H3 acetyltransferase activity / DNA replication-dependent chromatin assembly / acetyltransferase activator activity / nucleosome disassembly ...Formation of Senescence-Associated Heterochromatin Foci (SAHF) / H3 histone acetyltransferase complex / regulation of double-strand break repair via nonhomologous end joining / maintenance of rDNA / replication-born double-strand break repair via sister chromatid exchange / transposable element silencing / histone H3 acetyltransferase activity / DNA replication-dependent chromatin assembly / acetyltransferase activator activity / nucleosome disassembly / silent mating-type cassette heterochromatin formation / protein-lysine-acetyltransferase activity / histone H3K56 acetyltransferase activity / histone H3K23 acetyltransferase activity / histone H3K14 acetyltransferase activity / histone H3K9 acetyltransferase activity / cellular response to stress / histone H3K27 acetyltransferase activity / negative regulation of DNA damage checkpoint / subtelomeric heterochromatin formation / regulation of DNA repair / histone acetyltransferase / positive regulation of transcription elongation by RNA polymerase II / protein modification process / double-strand break repair via nonhomologous end joining / structural constituent of chromatin / nucleosome / protein transport / nucleosome assembly / chromatin organization / regulation of gene expression / histone binding / chromosome, telomeric region / protein heterodimerization activity / DNA damage response / chromatin binding / regulation of transcription by RNA polymerase II / chromatin / DNA binding / nucleoplasm / identical protein binding / nucleus / cytosol
Similarity search - Function
Histone acetyltransferase Rtt109 / : / Rtt109-type histone acetyltransferase (HAT) domain profile. / Histone deposition protein Asf1 / Nucleosome assembly protein (NAP) / NAP-like superfamily / Nucleosome assembly protein (NAP) / Histone chaperone ASF1-like / Histone chaperone ASF1-like superfamily / ASF1 like histone chaperone ...Histone acetyltransferase Rtt109 / : / Rtt109-type histone acetyltransferase (HAT) domain profile. / Histone deposition protein Asf1 / Nucleosome assembly protein (NAP) / NAP-like superfamily / Nucleosome assembly protein (NAP) / Histone chaperone ASF1-like / Histone chaperone ASF1-like superfamily / ASF1 like histone chaperone / Histone acetyltransferase Rtt109/CBP / Histone acetylation protein / Histone acetylation protein / TATA box binding protein associated factor / TATA box binding protein associated factor (TAF), histone-like fold domain / 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
Similarity search - Domain/homology
Histone chaperone ASF1 / Vacuolar protein sorting-associated protein 75 / Histone H4 / Histone H3.2 / Histone acetyltransferase RTT109
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Xenopus laevis (African clawed frog)
Contact author
  • Nataliya Danilenko (Leibniz University of Hannover, Germany)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Models

Model #3125
Type: atomic / Chi-square value: 0.696
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Complex with 1H histone chaperone Asf1, histones H3 (35-135aa) and H4; 70%-2H histone acetyltransferase Rtt109 and histone chaperone Vps75 (1-225aa) acquired in 100% v/v D2O
Specimen concentration: 2.55 mg/ml / Entity id: 1488 / 1489 / 1490 / 1491 / 1492
BufferName: 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O / pH: 6.5
Entity #1488Name: Vps75 1-225 / Type: protein
Description: Vacuolar protein sorting-associated protein 75 (1-225 aa)
Formula weight: 26.554 / Num. of mol.: 2
Source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
References: UniProt: P53853
Sequence: MMSDQENENE HAKAFLGLAK CEEEVDAIER EVELYRLNKM KPVYEKRDAY IDEIAEFWKI VLSQHVSFAN YIRASDFKYI DTIDKIKVEW LALESEMYDT RDFSITFHFH GIEGDFKEQQ VTKVFQIKKG KDDQEDGILT SEPVPIEWPQ SYDSINPDLI KDKRSPEGKK ...Sequence:
MMSDQENENE HAKAFLGLAK CEEEVDAIER EVELYRLNKM KPVYEKRDAY IDEIAEFWKI VLSQHVSFAN YIRASDFKYI DTIDKIKVEW LALESEMYDT RDFSITFHFH GIEGDFKEQQ VTKVFQIKKG KDDQEDGILT SEPVPIEWPQ SYDSINPDLI KDKRSPEGKK KYRQGMKTIF GWFRWTGLKP GKEFPHGDSL ASLFSEEIYP FCVKYYAEAQ RDLED
Entity #1489Name: Rtt109 / Type: protein / Description: Histone acetyltransferase RTT109 / Formula weight: 50.095 / Num. of mol.: 1
Source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
References: UniProt: Q07794
Sequence: MSLNDFLSSV LPVSEQFEYL SLQSIPLETH AVVTPNKDDK RVPKSTIKTQ HFFSLFHQGK VFFSLEVYVY VTLWDEADAE RLIFVSKADT NGYCNTRVSV RDITKIILEF ILSIDPNYYL QKVKPAIRSY KKISPELISA ASTPARTLRI LARRLKQSGS TVLKEIESPR ...Sequence:
MSLNDFLSSV LPVSEQFEYL SLQSIPLETH AVVTPNKDDK RVPKSTIKTQ HFFSLFHQGK VFFSLEVYVY VTLWDEADAE RLIFVSKADT NGYCNTRVSV RDITKIILEF ILSIDPNYYL QKVKPAIRSY KKISPELISA ASTPARTLRI LARRLKQSGS TVLKEIESPR FQQDLYLSFT CPREILTKIC LFTRPASQYL FPDSSKNSKK HILNGEELMK WWGFILDRLL IECFQNDTQA KLRIPGEDPA RVRSYLRGMK YPLWQVGDIF TSKENSLAVY NIPLFPDDPK ARFIHQLAEE DRLLKVSLSS FWIELQERQE FKLSVTSSVM GISGYSLATP SLFPSSADVI VPKSRKQFRA IKKYITGEEY DTEEGAIEAF TNIRDFLLLR MATNLQSLTG KREHRERNQP VPASNINTLA ITMLKPRKKA KALPKT
Entity #1490Name: Asf1 / Type: protein / Description: Histone chaperone ASF1 / Formula weight: 19.125 / Num. of mol.: 1 / References: UniProt: P32447
Sequence:
MSIVSLLGIK VLNNPAKFTD PYEFEITFEC LESLKHDLEW KLTYVGSSRS LDHDQELDSI LVGPVPVGVN KFVFSADPPS AELIPASELV SVTVILLSCS YDGREFVRVG YYVNNEYDEE ELRENPPAKV QVDHIVRNIL AEKPRVTRFN IVWDNENEGD LYPPEQPGV
Entity #1491Name: H3 (35-135) / Type: protein / Description: Histone H3.2 (35-135 aa) / Formula weight: 11.747 / Num. of mol.: 1 / Source: Xenopus laevis / References: UniProt: P84233
Sequence:
VKKPHRYRPG TVALREIRRY QKSTELLIRK LPFQRLVREI AQDFKTDLRF QSAAIGALQE ASEAYLVGLF EDTNLCAIHA KRVTIMPKDI QLARRIRGER A
Entity #1492Name: H4 / Type: protein / Description: Histone H4 / Formula weight: 11.367 / Num. of mol.: 1 / Source: Xenopus laevis / References: UniProt: P62799
Sequence:
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG

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Experimental information

BeamInstrument name: ILL D22 / City: Grenoble / 国: France / Type of source: neutron source / Wavelength: 0.6 Å / Dist. spec. to detc.: 4 mm
DetectorName: 128 linear sensitive Reuter-Stokes detector / Type: 3He multidetector / Pixsize x: 0.8 mm
Scan
Title: Complex with 1H histone chaperone Asf1, histones H3 (35-135aa) and H4; 70%-2H histone acetyltransferase Rtt109 and histone chaperone Vps75 (1-225aa) acquired in 100% v/v D2O
Measurement date: Nov 14, 2016 / Cell temperature: 25.1 °C / Exposure time: 3600 sec. / Number of frames: 1 / Unit: 1/A /
MinMax
Q0.0122 0.2405
Distance distribution function P(R)
Sofotware P(R): GNOM 4.6 / Number of points: 101 /
MinMax
Q0.01862 0.228
P(R) point4 104
R0 55
Result
Experimental MW: 145 kDa / Type of curve: single_conc
P(R)GuinierGuinier error
Forward scattering, I00.02038 0.02 0.00022
Radius of gyration, Rg2.06 nm1.943 nm0.036

MinMax
D-5.5
Guinier point1 27

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