[English] 日本語
Yorodumi
- PDB-4wju: Crystal structure of Rsa4 from Saccharomyces cerevisiae -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4wju
TitleCrystal structure of Rsa4 from Saccharomyces cerevisiae
ComponentsRibosome assembly protein 4
KeywordsBIOSYNTHETIC PROTEIN / ribosome biogenesis ribosome assembly
Function / homology
Function and homology information


protein-RNA complex remodeling / Antigen processing: Ubiquitination & Proteasome degradation / ribosomal large subunit assembly / nucleolus
Similarity search - Function
NLE / NLE (NUC135) domain / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. ...NLE / NLE (NUC135) domain / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
Ribosome assembly protein 4
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å
AuthorsHoldermann, I. / Bassler, J. / Hurt, E. / Sinning, I.
CitationJournal: J.Cell Biol. / Year: 2014
Title: A network of assembly factors is involved in remodeling rRNA elements during preribosome maturation.
Authors: Baler, J. / Paternoga, H. / Holdermann, I. / Thoms, M. / Granneman, S. / Barrio-Garcia, C. / Nyarko, A. / Stier, G. / Clark, S.A. / Schraivogel, D. / Kallas, M. / Beckmann, R. / Tollervey, D. ...Authors: Baler, J. / Paternoga, H. / Holdermann, I. / Thoms, M. / Granneman, S. / Barrio-Garcia, C. / Nyarko, A. / Stier, G. / Clark, S.A. / Schraivogel, D. / Kallas, M. / Beckmann, R. / Tollervey, D. / Barbar, E. / Sinning, I. / Hurt, E.
History
DepositionOct 1, 2014Deposition site: RCSB / Processing site: PDBE
Revision 1.0Nov 19, 2014Provider: repository / Type: Initial release
Revision 1.1Dec 3, 2014Group: Database references
Revision 1.2Dec 10, 2014Group: Database references
Revision 1.3Jan 14, 2015Group: Database references
Revision 1.4Jan 10, 2024Group: 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

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Ribosome assembly protein 4
B: Ribosome assembly protein 4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)114,3063
Polymers114,2142
Non-polymers921
Water0
1
A: Ribosome assembly protein 4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)57,1992
Polymers57,1071
Non-polymers921
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Ribosome assembly protein 4


Theoretical massNumber of molelcules
Total (without water)57,1071
Polymers57,1071
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)96.870, 108.470, 261.910
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number23
Space group name H-MI222

-
Components

#1: Protein Ribosome assembly protein 4 / Notchless protein homolog 1 / Ribosome biogenesis factor RSA4 / Ribosome assembly protein 4


Mass: 57106.781 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c / Gene: RSA4, YCR072C, YCR72C / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P25382
#2: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Formula: C3H8O3
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Strain: ATCC 204508 / S288c / Gene: RSA4, YCR072C, YCR72C / Production host: Escherichia coli BL21(DE3) (bacteria)

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION

-
Sample preparation

CrystalDensity Matthews: 3.42 Å3/Da / Density % sol: 64.06 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / Details: 3.5M NaHCO2, 2.25M NH4Ac

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-2 / Wavelength: 1 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Nov 22, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.8→43.61 Å / Num. obs: 33508 / % possible obs: 97.26 % / Redundancy: 1.9 % / Rmerge(I) obs: 0.094 / Net I/σ(I): 7.68
Reflection shellResolution: 2.8→2.9 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.47 / Mean I/σ(I) obs: 2.25 / % possible all: 98.6

-
Processing

Software
NameVersionClassification
PHENIX(phenix.refine: 1.8.4_1496)refinement
XDSdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4WJS
Resolution: 2.8→43.609 Å / SU ML: 0.37 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 25.96 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2461 1999 5.97 %
Rwork0.2034 --
obs0.206 33498 97.23 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.8→43.609 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7055 0 6 0 7061
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0057228
X-RAY DIFFRACTIONf_angle_d0.8619792
X-RAY DIFFRACTIONf_dihedral_angle_d15.1612600
X-RAY DIFFRACTIONf_chiral_restr0.0341088
X-RAY DIFFRACTIONf_plane_restr0.0041220
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.8-2.870.36571420.31462242X-RAY DIFFRACTION98
2.87-2.94760.33551440.30092256X-RAY DIFFRACTION98
2.9476-3.03430.34791420.28732245X-RAY DIFFRACTION98
3.0343-3.13220.33491410.2692229X-RAY DIFFRACTION98
3.1322-3.24410.2981430.25172246X-RAY DIFFRACTION98
3.2441-3.3740.30061410.22792226X-RAY DIFFRACTION97
3.374-3.52750.23891420.20132234X-RAY DIFFRACTION98
3.5275-3.71330.25051420.19032247X-RAY DIFFRACTION98
3.7133-3.94590.21661430.17962260X-RAY DIFFRACTION98
3.9459-4.25030.21751430.16322241X-RAY DIFFRACTION97
4.2503-4.67760.17961420.13752239X-RAY DIFFRACTION97
4.6776-5.35340.1611440.14682266X-RAY DIFFRACTION97
5.3534-6.74070.23411440.19782264X-RAY DIFFRACTION96
6.7407-43.61410.23521460.20792304X-RAY DIFFRACTION94
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)
15.54921.24650.60933.7545-0.33426.2242-0.52430.4050.2107-0.7484-0.0316-0.0629-0.2527-0.31590.45221.1467-0.1898-0.11271.0720.08880.584-24.3346-30.1688-54.9978
21.89850.1718-1.4191.2483-0.03052.32840.03260.80330.194-0.5529-0.00610.0613-0.7532-0.0702-0.05810.5869-0.1103-0.10760.7370.1430.4151-34.6287-26.1207-39.4115
31.6688-0.4171-0.10180.88560.16741.4445-0.02630.2876-0.0355-0.08410.03210.03330.0217-0.1393-0.01610.1533-0.0570.00830.21250.03520.1999-34.4573-44.8037-14.2002
43.2109-0.49580.3841.1075-0.70511.73780.01440.37230.258-0.09220.0537-0.0022-0.14080.1561-0.03950.2563-0.0976-0.00750.34920.07690.2461-24.976-30.0334-23.3436
52.86141.01440.38560.9680.32990.1182-0.3575-0.425-0.46730.15330.1-0.1432-0.39890.03660.17551.1726-0.19790.16761.2672-0.06910.5669-25.8638-26.074757.2774
61.09640.55550.66882.572-1.06261.21180.1632-0.60040.00970.7582-0.11050.1613-0.3482-1.3534-0.05831.0235-0.09580.15541.1331-0.27550.513-26.5747-20.455149.1377
71.91850.1680.03721.70440.09842.91590.0512-0.21540.25980.11830.0735-0.1303-0.27750.4223-0.09730.2642-0.02050.0220.2701-0.12560.278-9.1471-27.759318.6233
85.00730.8008-0.39545.95031.0122.4957-0.1022-0.5118-0.21960.36960.17690.6764-0.17-0.66350.00320.2540.03780.03030.5042-0.05410.3118-28.9064-30.583824.723
92.43370.2749-0.04061.20990.1091.26180.1856-0.4760.64840.0573-0.20910.3155-0.7102-0.27010.04060.57540.03590.05950.4662-0.21440.4981-21.6716-12.851127.6586
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 33 through 102 )
2X-RAY DIFFRACTION2chain 'A' and (resid 103 through 145 )
3X-RAY DIFFRACTION3chain 'A' and (resid 146 through 364 )
4X-RAY DIFFRACTION4chain 'A' and (resid 365 through 515 )
5X-RAY DIFFRACTION5chain 'B' and (resid 30 through 76 )
6X-RAY DIFFRACTION6chain 'B' and (resid 77 through 133 )
7X-RAY DIFFRACTION7chain 'B' and (resid 134 through 364 )
8X-RAY DIFFRACTION8chain 'B' and (resid 365 through 410 )
9X-RAY DIFFRACTION9chain 'B' and (resid 411 through 515 )

+
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://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