[English] 日本語
Yorodumi
- PDB-4wkr: LaRP7 wrapping up the 3' hairpin of 7SK non-coding RNA (302-332) -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4wkr
TitleLaRP7 wrapping up the 3' hairpin of 7SK non-coding RNA (302-332)
Components
  • 7SK GGHP4 (300-332)
  • La-related protein 7
KeywordsRNA BINDING PROTEIN / RNA-BINDING PROTEIN / RNA RECOGNITION MOTIF / PHOSPHOPROTEIN / PROTEIN / NUCLEUS / LA MOTIF
Function / homology
Function and homology information


U6 2'-O-snRNA methylation / 7SK snRNP / positive regulation of snRNA transcription by RNA polymerase II / 7SK snRNA binding / box C/D sno(s)RNA 3'-end processing / positive regulation of protein localization to Cajal body / : / negative regulation of viral transcription / regulation of mRNA splicing, via spliceosome / negative regulation of transcription elongation by RNA polymerase II ...U6 2'-O-snRNA methylation / 7SK snRNP / positive regulation of snRNA transcription by RNA polymerase II / 7SK snRNA binding / box C/D sno(s)RNA 3'-end processing / positive regulation of protein localization to Cajal body / : / negative regulation of viral transcription / regulation of mRNA splicing, via spliceosome / negative regulation of transcription elongation by RNA polymerase II / U6 snRNA binding / RNA splicing / mRNA processing / spermatogenesis / cell differentiation / ribonucleoprotein complex / mRNA binding / negative regulation of transcription by RNA polymerase II / RNA binding / nucleoplasm / nucleus / cytosol
Similarity search - Function
LARP7, RNA recognition motif 1 / LARP7, RNA recognition motif 2 / La-related protein 7, La domain / RNA binding motif / Lupus La protein / xRRM domain profile. / La protein, xRRM domain / La domain containing protein / La domain / Domain in the RNA-binding Lupus La protein; unknown function ...LARP7, RNA recognition motif 1 / LARP7, RNA recognition motif 2 / La-related protein 7, La domain / RNA binding motif / Lupus La protein / xRRM domain profile. / La protein, xRRM domain / La domain containing protein / La domain / Domain in the RNA-binding Lupus La protein; unknown function / La-type HTH domain / La-type HTH domain profile. / RRM (RNA recognition motif) domain / RNA recognition motif / RNA recognition motif / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif domain / Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain / RNA-binding domain superfamily / Arc Repressor Mutant, subunit A / Winged helix DNA-binding domain superfamily / Nucleotide-binding alpha-beta plait domain superfamily / Alpha-Beta Plaits / Winged helix-like DNA-binding domain superfamily / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
RNA / RNA (> 10) / La-related protein 7
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.2 Å
AuthorsUchikawa, E. / Natchiar, K.S. / Han, X. / Proux, F. / Roblin, P. / Zhang, E. / Durand, A. / Klaholz, B.P. / Dock-Bregeon, A.-C.
CitationJournal: Nucleic Acids Res. / Year: 2015
Title: Structural insight into the mechanism of stabilization of the 7SK small nuclear RNA by LARP7.
Authors: Uchikawa, E. / Natchiar, K.S. / Han, X. / Proux, F. / Roblin, P. / Zhang, E. / Durand, A. / Klaholz, B.P. / Dock-Bregeon, A.C.
History
DepositionOct 3, 2014Deposition site: RCSB / Processing site: PDBE
Revision 1.0Mar 18, 2015Provider: repository / Type: Initial release
Revision 1.1Apr 15, 2015Group: Database references
Revision 1.2Jan 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: La-related protein 7
B: La-related protein 7
C: 7SK GGHP4 (300-332)
D: 7SK GGHP4 (300-332)


Theoretical massNumber of molelcules
Total (without water)67,7174
Polymers67,7174
Non-polymers00
Water905
1
A: La-related protein 7
C: 7SK GGHP4 (300-332)


Theoretical massNumber of molelcules
Total (without water)33,8582
Polymers33,8582
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: La-related protein 7
D: 7SK GGHP4 (300-332)


Theoretical massNumber of molelcules
Total (without water)33,8582
Polymers33,8582
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)163.452, 33.500, 119.080
Angle α, β, γ (deg.)90.00, 128.99, 90.00
Int Tables number5
Space group name H-MC121

-
Components

#1: Protein La-related protein 7 / La ribonucleoprotein domain family member 7 / P-TEFb-interaction protein for 7SK stability / PIP7S


Mass: 24022.566 Da / Num. of mol.: 2 / Fragment: N-TERMINAL DOMAIN, UNP Residues 1-208
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: LARP7, HDCMA18P / Plasmid: PET15 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): Rosetta / References: UniProt: Q4G0J3
#2: RNA chain 7SK GGHP4 (300-332)


Mass: 9835.749 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION

-
Sample preparation

CrystalDensity Matthews: 3.17 Å3/Da / Density % sol: 61.17 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7 / Details: 30% PEG 3350 & 0.1 M succinic acid, pH 7.0 / PH range: 7

-
Data collection

DiffractionMean temperature: 140 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Dec 18, 2012
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.2→92.58 Å / Num. all: 27542 / Num. obs: 8165 / % possible obs: 95.2 % / Redundancy: 3.4 % / Biso Wilson estimate: 106.93 Å2 / Net I/σ(I): 5.41
Reflection shellResolution: 3.2→3.5 Å / Redundancy: 3.4 % / Mean I/σ(I) obs: 2 / % possible all: 94.9

-
Processing

Software
NameVersionClassification
BUSTER2.10.0refinement
iMOSFLMdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2VOO
Resolution: 3.2→59.06 Å / Cor.coef. Fo:Fc: 0.919 / Cor.coef. Fo:Fc free: 0.9051 / Cross valid method: FREE R-VALUE / σ(F): 0 / SU Rfree Blow DPI: 0.505
RfactorNum. reflection% reflectionSelection details
Rfree0.274 382 4.68 %RANDOM
Rwork0.2206 ---
obs0.2232 8155 94.04 %-
Displacement parametersBiso mean: 93.76 Å2
Baniso -1Baniso -2Baniso -3
1--7.9841 Å20 Å2-14.7608 Å2
2--6.3558 Å20 Å2
3---1.6283 Å2
Refine analyzeLuzzati coordinate error obs: 0.707 Å
Refinement stepCycle: 1 / Resolution: 3.2→59.06 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2522 168 0 5 2695
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.012749HARMONIC2
X-RAY DIFFRACTIONt_angle_deg1.323743HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d990SINUSOIDAL2
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes63HARMONIC2
X-RAY DIFFRACTIONt_gen_planes386HARMONIC5
X-RAY DIFFRACTIONt_it2749HARMONIC20
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_omega_torsion2.73
X-RAY DIFFRACTIONt_other_torsion24.14
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_chiral_improper_torsion366SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact3109SEMIHARMONIC4
LS refinement shellResolution: 3.2→3.58 Å / Total num. of bins used: 5
RfactorNum. reflection% reflection
Rfree0.3076 111 4.92 %
Rwork0.257 2146 -
all0.2596 2257 -
obs--94.04 %

+
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