[English] 日本語
Yorodumi
- PDB-3q68: Structure of the Vps75-Rtt109 histone chaperone-lysine acetyltran... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 3q68
TitleStructure of the Vps75-Rtt109 histone chaperone-lysine acetyltransferase complex (Full-length proteins in space group P212121)
Components
  • Histone acetyltransferase RTT109
  • Vacuolar protein sorting-associated protein 75 (VPS75)
KeywordsCHAPERONE/TRANSFERASE / Histone chaperone / Lysine acetyltransferase / CHAPERONE-TRANSFERASE complex
Function / homology
Function and homology information


histone H3K23 acetyltransferase activity / histone H3K56 acetyltransferase activity / H3 histone acetyltransferase complex / DNA replication-dependent chromatin disassembly / histone H3K14 acetyltransferase activity / regulation of double-strand break repair via nonhomologous end joining / histone H3K9 acetyltransferase activity / maintenance of rDNA / acetyltransferase activator activity / replication-born double-strand break repair via sister chromatid exchange ...histone H3K23 acetyltransferase activity / histone H3K56 acetyltransferase activity / H3 histone acetyltransferase complex / DNA replication-dependent chromatin disassembly / histone H3K14 acetyltransferase activity / regulation of double-strand break repair via nonhomologous end joining / histone H3K9 acetyltransferase activity / maintenance of rDNA / acetyltransferase activator activity / replication-born double-strand break repair via sister chromatid exchange / retrotransposon silencing / histone H3 acetyltransferase activity / histone H3K27 acetyltransferase activity / peptide-lysine-N-acetyltransferase activity / histone acetyltransferase / protein modification process / double-strand break repair via nonhomologous end joining / nucleosome assembly / protein transport / histone binding / regulation of gene expression / DNA damage response / chromatin binding / chromatin / regulation of transcription by RNA polymerase II / identical protein binding / nucleus / cytosol
Similarity search - Function
Histone acetyltransferase Rtt109 / Rtt109-type histone acetyltransferase (HAT) domain profile. / Nucleosome assembly protein (NAP) / NAP-like superfamily / Nucleosome assembly protein (NAP) / Histone acetyltransferase Rtt109/CBP / Histone acetylation protein / Histone acetylation protein
Similarity search - Domain/homology
Vacuolar protein sorting-associated protein 75 / Histone acetyltransferase RTT109
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.705 Å
AuthorsSu, D. / Thompson, J.R. / Mer, G.
CitationJournal: J.Biol.Chem. / Year: 2011
Title: Structure and histone binding properties of the Vps75-Rtt109 chaperone-lysine acetyltransferase complex.
Authors: Su, D. / Hu, Q. / Zhou, H. / Thompson, J.R. / Xu, R.M. / Zhang, Z. / Mer, G.
History
DepositionDec 30, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 23, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Sep 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details
Revision 1.3Dec 6, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Vacuolar protein sorting-associated protein 75 (VPS75)
C: Histone acetyltransferase RTT109
B: Vacuolar protein sorting-associated protein 75 (VPS75)


Theoretical massNumber of molelcules
Total (without water)112,1193
Polymers112,1193
Non-polymers00
Water1,62190
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8190 Å2
ΔGint-52 kcal/mol
Surface area41620 Å2
MethodPISA
Unit cell
Length a, b, c (Å)90.988, 98.056, 171.366
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

-
Components

#1: Protein Vacuolar protein sorting-associated protein 75 (VPS75)


Mass: 30656.084 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: VPS75, YNL246W, N0890 / Plasmid: pCOLA Duet-1 / Production host: Escherichia coli (E. coli) / References: UniProt: P53853
#2: Protein Histone acetyltransferase RTT109 / Regulator of Ty1 transposition protein 109


Mass: 50806.461 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: RTT109, KIM2, REM50, YLL002W, L1377 / Plasmid: GST-based pET / Production host: Escherichia coli (E. coli) / References: UniProt: Q07794, histone acetyltransferase
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 90 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 3.41 Å3/Da / Density % sol: 63.92 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 1.8 M sodium citrate, 30% (w/v) 1,6-hexanediol, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97901 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Nov 29, 2009
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97901 Å / Relative weight: 1
ReflectionResolution: 2.7→50 Å / Num. obs: 40782 / % possible obs: 99.6 % / Redundancy: 8.1 % / Rmerge(I) obs: 0.072 / Net I/σ(I): 28.4
Reflection shellResolution: 2.7→2.75 Å / Redundancy: 8.3 % / Rmerge(I) obs: 0.904 / Mean I/σ(I) obs: 2.5 / % possible all: 100

-
Processing

Software
NameVersionClassification
HKL-3000data collection
PHASERphasing
PHENIX(phenix.refine: 1.6.1_357)refinement
HKL-3000data reduction
HKL-3000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entries 3CZ7 2ZD7
Resolution: 2.705→47.137 Å / SU ML: 0.36 / σ(F): 0.1 / Phase error: 24.2 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2258 510 1.25 %
Rwork0.2016 --
obs0.202 40782 95.65 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 65.472 Å2 / ksol: 0.389 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--3.2534 Å2-0 Å20 Å2
2---4.1551 Å2-0 Å2
3---7.4085 Å2
Refinement stepCycle: LAST / Resolution: 2.705→47.137 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7055 0 0 90 7145
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0227225
X-RAY DIFFRACTIONf_angle_d1.5459752
X-RAY DIFFRACTIONf_dihedral_angle_d16.2062736
X-RAY DIFFRACTIONf_chiral_restr0.1211039
X-RAY DIFFRACTIONf_plane_restr0.0121251
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.7047-2.97690.31271110.26569227X-RAY DIFFRACTION89
2.9769-3.40750.24711160.2310017X-RAY DIFFRACTION96
3.4075-4.29270.23331510.174310379X-RAY DIFFRACTION99
4.2927-47.14390.19131320.193710649X-RAY DIFFRACTION98
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
13.8563.3351-1.56663.0597-1.7916.06230.1692-0.2321.2006-0.04430.37330.90110.43110.3068-0.45810.58350.01610.19060.9273-0.01280.714123.5739-0.01-9.675
2-0.0425-0.40930.0659.89181.20090.3891-0.2073-0.08-0.09610.1270.604-1.8460.08990.3007-0.37020.2301-0.14640.06290.7504-0.19930.530815.321425.3078-4.7525
33.12110.14581.65241.12210.57440.8533-0.20360.01030.38160.1461-0.1290.0806-0.2320.0120.25650.3957-0.00520.05310.3644-0.0030.354810.013741.636317.073
43.18893.3251.01536.1027-1.50752.81511.11511.0805-1.10430.0017-0.7036-0.9035-0.8218-0.5938-0.06640.3747-0.0507-0.0610.5459-0.0520.497819.551238.26570.6538
52.76990.45580.38370.4898-0.46380.53530.14580.440.44890.135-0.1274-0.1621-0.13870.17690.04830.4119-0.10250.03960.39530.11490.299921.096543.298612.4932
64.3132-0.9797-0.16021.3460.26310.019-0.4474-0.20620.48-0.34550.1370.35610.26960.11810.19640.51060.08890.13620.6677-0.07410.364831.065123.71945.7176
71.78151.60811.53861.9340.49482.5942-0.01620.10620.37140.0911-0.058-0.0977-0.34620.90310.06580.4599-0.233-0.10160.6118-0.01040.475829.969545.006626.6902
85.3173.26682.96178.17511.30413.38040.8118-0.3634-1.15470.5573-0.6825-2.5103-0.00010.3146-0.09370.4857-0.0765-0.16870.62650.19421.043932.7235.949233.1058
91.1711.79421.4695.23210.30463.5894-0.03470.0703-0.43660.22460.0573-0.61740.1230.31610.0240.3065-0.1060.02090.59170.0050.333328.181334.572620.2178
105.986-3.2606-1.02432.05820.93482.0609-0.23530.4311-1.1397-0.1718-0.02110.4726-0.1729-0.27650.23050.3481-0.01670.02080.3615-0.02490.48336.970534.413214.5659
113.59490.9834-0.51162.16890.35751.00960.0122-0.243-0.530.22750.20920.08970.00140.0028-0.17060.3511-0.0751-0.03640.3904-0.02230.6485-4.033430.435323.4127
124.8318-3.19684.68362.1291-3.13864.58441.76420.54940.741-2.2678-2.1152-0.32772.94910.7079-0.06431.44770.2522-0.43770.7082-0.10031.2155-8.4744.699722.6284
131.7841-0.27320.41432.2651-0.77310.6350.2633-0.38130.05520.5985-0.14910.1999-0.2195-0.115-0.09970.6198-0.07940.17040.4229-0.0390.31854.421727.974949.6103
140.93370.0532-1.59790.0001-0.1956.06330.2616-0.07750.37720.02770.58050.4988-0.91530.2396-0.72370.49480.0442-0.34080.2985-0.05280.9403-12.80035.453230.9423
154.0491-1.8492-2.58693.3566-1.18383.8558-0.57511.9352-4.6907-0.09940.0185-0.7729-1.1522-0.70440.30820.7839-0.1543-0.1691.4539-0.01581.501-19.96325.256435.8613
160.4692-0.11120.04862.174-0.4592-0.00760.13940.08520.18180.4423-0.44190.0719-0.2454-0.00630.14680.53140.02130.07070.4255-0.01370.36276.33623.471141.924
170.79040.60780.13370.6801-0.25930.9864-0.1599-0.1614-0.4097-0.00390.3082-0.00280.4371-0.1502-0.06560.5823-0.06950.09460.29150.00150.5393-11.339513.526341.1596
181.95580.4913-1.89163.1443-1.13817.258-0.50020.1399-0.3471-0.4004-0.2555-0.7364-0.69830.6342-0.5590.5651-0.0167-0.12690.33990.17030.326817.748120.571246.5241
190.69830.90530.52771.3456-0.43090.59630.43880.02730.11870.1855-0.29220.49680.0066-0.0629-0.15410.5794-0.0290.12140.3072-0.06490.4152-4.371822.717543.2777
207.4453-0.1579-3.90820.21040.40252.41880.38030.03271.6281-0.20160.7610.74020.37810.1484-1.13770.44020.0517-0.07531.31580.02970.8579-20.759134.201419.4063
210.5022-0.3728-0.55952.0357-0.85592.53930.2190.2371-0.49790.0860.0171.0265-0.3302-0.9786-0.16170.32070.1109-0.01020.5229-0.05480.392-11.150741.342915.6668
223.6114-3.056-1.24698.51550.64047.3965-1.0933-0.2999-0.5657-0.08662.5353-0.1595-0.2378-0.3579-0.71090.62110.06040.18621.4094-0.27390.8106-19.373536.154130.4954
230.74651.47220.07914.6524-1.72850.70940.420.12310.0807-0.1144-0.2330.12140.2068-0.175-0.14070.4918-0.01640.0720.429-0.10.458-3.807815.230741.6814
241.7398-0.35060.77482.456-1.26360.94450.2849-0.1844-0.05540.438-0.3032-0.18840.04660.27460.02660.5731-0.1181-0.00520.43180.05190.394810.04559.156348.8528
255.514.02952.01483.1311.16211.8284-0.13640.7812-1.51651.2302-0.1235-1.6290.24380.57690.39460.594-0.10550.19960.54850.15911.07628.6105-6.699152.4357
262.86090.44153.48930.7367-1.43026.91730.60710.0133-0.8505-0.13380.09780.13240.3216-0.0667-0.58630.6846-0.0687-0.06920.4083-0.02660.5243-4.6573-0.467144.8313
273.167-1.3170.91213.53261.06633.49850.77550.4875-0.175-0.6576-0.40850.27650.8620.7648-0.23320.84850.30230.0540.4825-0.05370.49521.2756-1.629830.1379
280.68421.0906-0.24242.96070.1704-0.0180.06110.02760.20820.3439-0.1623-0.37430.0607-0.02810.0490.55510.01790.09940.4507-0.01190.49940.625214.605445.5139
293.37140.2021-0.86661.44871.05080.90920.21270.5901-0.5326-0.0559-0.1924-0.1477-0.36520.0460.03950.52810.00590.10550.39450.01360.444812.593927.28832.7387
301.15330.17950.22663.5481-0.27710.39060.1430.07730.1670.5975-0.353-0.1791-0.23590.0520.1260.6156-0.1247-0.01990.40180.0530.408512.221634.931543.0043
310.84710.1505-0.51456.02551.68443.0481-0.00570.2438-0.00680.13760.2650.2151-0.52950.5592-0.19720.61840.0016-0.0130.66570.04410.4958-4.605149.89269.296
320.2986-0.3472-0.64311.66590.93591.2327-0.09570.6461-0.1517-0.2905-0.48880.375-0.1125-0.37030.52440.2717-0.1132-0.02010.6149-0.02860.45555.800823.3693-5.9654
336.1819-1.6681.39840.94910.03620.688-0.1574-0.4235-1.8111-0.3580.89680.39530.06510.0612-0.43370.60820.00830.15450.9159-0.06241.220813.3698-0.3237-5.7275
341.57450.7134-2.72470.7702-1.20765.75990.301-0.82480.1395-0.17740.1742-0.04090.94141.1922-0.1410.92310.1754-0.15540.97440.11980.73544.6484-2.532310.3833
353.13310.4241-1.08610.635-0.66390.4714-0.48710.2948-0.0713-0.29170.3643-0.03130.158-0.22080.11940.4428-0.11640.00610.6274-0.14310.4033-0.982.788-4.3695
365.4366-4.6285-2.97163.92432.50554.1961.005-0.08273.1624-1.95780.6239-1.75780.68660.0771-1.28710.61680.167-0.10430.3214-0.00231.3292-12.590524.62227.6367
370.10210.3676-0.53852.8311-1.1691.1563-0.31710.3651-0.4542-0.16140.55660.99450.1028-1.005-0.15340.2175-0.22490.00810.7069-0.1370.776-11.0051-6.43063.0882
382.74760.46952.74762.23270.87072.925-1.60311.0612-1.00290.05440.85790.1632-0.54320.20410.58381.02230.04190.46041.0060.29181.0648-18.1659-9.66515.8469
390.73180.7986-1.34632.7492-0.4272.1277-0.9131-0.4491-0.13230.04070.4724-0.34710.17810.45990.32530.48340.05840.12620.74520.09490.7235-9.59210.66828.4063
401.201-0.5165-2.00484.34780.36893.3429-0.5519-1.07780.8281-0.0990.3064-1.03080.08820.86150.27610.33590.0732-0.08280.7142-0.06160.59047.76187.06873.1016
415.8359-6.1377-1.50946.56691.07843.35290.37582.1979-0.26480.2475-0.1281-2.16430.3251-0.7526-0.18460.71840.1124-0.34531.0726-0.43722.009922.0666-0.95666.3434
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(chain A and resid 2:20)
2X-RAY DIFFRACTION2(chain A and resid 21:42)
3X-RAY DIFFRACTION3(chain A and resid 43:86)
4X-RAY DIFFRACTION4(chain A and resid 87:95)
5X-RAY DIFFRACTION5(chain A and resid 96:125)
6X-RAY DIFFRACTION6(chain A and resid 126:140)
7X-RAY DIFFRACTION7(chain A and resid 141:163)
8X-RAY DIFFRACTION8(chain A and resid 164:177)
9X-RAY DIFFRACTION9(chain A and resid 178:197)
10X-RAY DIFFRACTION10(chain A and resid 198:223)
11X-RAY DIFFRACTION11(chain A and resid 224:231)
12X-RAY DIFFRACTION12(chain A and resid 247:253)
13X-RAY DIFFRACTION13(chain B and resid -1:29)
14X-RAY DIFFRACTION14(chain B and resid 30:38)
15X-RAY DIFFRACTION15(chain B and resid 39:43)
16X-RAY DIFFRACTION16(chain B and resid 44:67)
17X-RAY DIFFRACTION17(chain B and resid 68:84)
18X-RAY DIFFRACTION18(chain B and resid 85:98)
19X-RAY DIFFRACTION19(chain B and resid 99:130)
20X-RAY DIFFRACTION20(chain B and resid 131:136)
21X-RAY DIFFRACTION21(chain B and resid 137:166)
22X-RAY DIFFRACTION22(chain B and resid 167:174)
23X-RAY DIFFRACTION23(chain B and resid 175:199)
24X-RAY DIFFRACTION24(chain B and resid 200:246)
25X-RAY DIFFRACTION25(chain B and resid 247:257)
26X-RAY DIFFRACTION26(chain B and resid 258:284)
27X-RAY DIFFRACTION27(chain B and resid 285:319)
28X-RAY DIFFRACTION28(chain B and resid 320:352)
29X-RAY DIFFRACTION29(chain B and resid 353:374)
30X-RAY DIFFRACTION30(chain B and resid 375:403)
31X-RAY DIFFRACTION31(chain C and resid 3:22)
32X-RAY DIFFRACTION32(chain C and resid 23:44)
33X-RAY DIFFRACTION33(chain C and resid 45:62)
34X-RAY DIFFRACTION34(chain C and resid 63:77)
35X-RAY DIFFRACTION35(chain C and resid 78:128)
36X-RAY DIFFRACTION36(chain C and resid 129:137)
37X-RAY DIFFRACTION37(chain C and resid 138:161)
38X-RAY DIFFRACTION38(chain C and resid 162:172)
39X-RAY DIFFRACTION39(chain C and resid 173:196)
40X-RAY DIFFRACTION40(chain C and resid 197:216)
41X-RAY DIFFRACTION41(chain C and resid 217:223)

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbjlvh1.pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more