[English] 日本語
Yorodumi
- PDB-3gvt: Structure and RNA binding of the mouse Pumilio-2 Puf Domain -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 3gvt
TitleStructure and RNA binding of the mouse Pumilio-2 Puf Domain
ComponentsPumilio homolog 2
KeywordsRNA BINDING PROTEIN / RNA-binding / Pumilio / Puf domain
Function / homology
Function and homology information


positive regulation of sprouting of injured axon / pumilio-response element binding / regulation of intracellular mRNA localization / positive regulation of miRNA-mediated gene silencing / regulation of chromosome segregation / positive regulation of RIG-I signaling pathway / miRNA processing / lncRNA binding / miRNA binding / post-transcriptional regulation of gene expression ...positive regulation of sprouting of injured axon / pumilio-response element binding / regulation of intracellular mRNA localization / positive regulation of miRNA-mediated gene silencing / regulation of chromosome segregation / positive regulation of RIG-I signaling pathway / miRNA processing / lncRNA binding / miRNA binding / post-transcriptional regulation of gene expression / hair follicle development / chromosome organization / adipose tissue development / stress granule assembly / regulation of mRNA stability / respiratory electron transport chain / mitochondrion organization / skeletal system development / mRNA 3'-UTR binding / cytoplasmic stress granule / regulation of translation / nuclear membrane / negative regulation of gene expression / neuronal cell body / perinuclear region of cytoplasm / RNA binding / cytoplasm / cytosol
Similarity search - Function
Pumilio, RNA binding domain / Pumilio homology domain / Pumilio homology domain (PUM-HD) profile. / Pumilio-family RNA binding repeat / Pumilio RNA-binding repeat profile. / Pumilio RNA-binding repeat / Pumilio-like repeats / Leucine-rich Repeat Variant / Leucine-rich Repeat Variant / Armadillo-like helical ...Pumilio, RNA binding domain / Pumilio homology domain / Pumilio homology domain (PUM-HD) profile. / Pumilio-family RNA binding repeat / Pumilio RNA-binding repeat profile. / Pumilio RNA-binding repeat / Pumilio-like repeats / Leucine-rich Repeat Variant / Leucine-rich Repeat Variant / Armadillo-like helical / Alpha Horseshoe / Armadillo-type fold / Mainly Alpha
Similarity search - Domain/homology
2,3-DIHYDROXY-1,4-DITHIOBUTANE / Pumilio homolog 2
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å
AuthorsJenkins, H.T. / Edwards, T.A.
CitationJournal: J.Struct.Biol. / Year: 2009
Title: Structure and RNA binding of the mouse Pumilio-2 Puf domain
Authors: Jenkins, H.T. / Baker-Wilding, R. / Edwards, T.A.
History
DepositionMar 31, 2009Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Jun 30, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Refinement description / Version format compliance
Revision 1.2Nov 1, 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_ncs_dom_lim / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Pumilio homolog 2
B: Pumilio homolog 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)81,2445
Polymers80,9052
Non-polymers3383
Water1,54986
1
A: Pumilio homolog 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)40,7914
Polymers40,4531
Non-polymers3383
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Pumilio homolog 2


Theoretical massNumber of molelcules
Total (without water)40,4531
Polymers40,4531
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)150.540, 150.540, 77.220
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number173
Space group name H-MP63
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B

NCS domain segments:

Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: GLY / Beg label comp-ID: GLY / End auth comp-ID: LEU / End label comp-ID: LEU / Refine code: 2 / Auth seq-ID: 706 - 1049 / Label seq-ID: 3 - 344

Dom-IDAuth asym-IDLabel asym-ID
1AA
2BB

-
Components

#1: Protein Pumilio homolog 2 / Pumilio 2


Mass: 40452.551 Da / Num. of mol.: 2 / Fragment: Puf domain, UNP residues 706-1056
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Pum2 / Plasmid: pET-19b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: Q80U58
#2: Chemical ChemComp-DTT / 2,3-DIHYDROXY-1,4-DITHIOBUTANE / 1,4-DITHIOTHREITOL


Mass: 154.251 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H10O2S2
#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 86 / Source method: isolated from a natural source / Formula: H2O
Sequence detailsTHE SEQUENCE OF THIS ENTITY BASED ON THE ISOFORM 2 OF UNIPROTKB/SUISS-PROT Q80U58 (PUM2_MOUSE). ...THE SEQUENCE OF THIS ENTITY BASED ON THE ISOFORM 2 OF UNIPROTKB/SUISS-PROT Q80U58 (PUM2_MOUSE). RESIDUES 829 VAL AND 830 ILE WERE MISSING IN ISOFORM 2.

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 3.12 Å3/Da / Density % sol: 60.6 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 0.2M ammonium citrate, 0.2M Li2SO4, 22%(w/v) PEG 4000 , pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.92 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Mar 11, 2008
RadiationMonochromator: Si (111) double crystal monochromator. / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.92 Å / Relative weight: 1
ReflectionResolution: 2.8→37.88 Å / Num. all: 24770 / Num. obs: 24746 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 5.7 / Redundancy: 5.4 % / Biso Wilson estimate: 75.5 Å2 / Rmerge(I) obs: 0.089 / Net I/σ(I): 11.5
Reflection shellResolution: 2.8→2.95 Å / Redundancy: 5.5 % / Rmerge(I) obs: 0.471 / Mean I/σ(I) obs: 5.7 / Num. unique all: 3595 / % possible all: 100

-
Processing

Software
NameVersionClassification
ADSCQuantumdata collection
PHASERphasing
REFMAC5.2.0019refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3GVO
Resolution: 2.8→37.87 Å / Cor.coef. Fo:Fc: 0.948 / Cor.coef. Fo:Fc free: 0.902 / SU B: 27.668 / SU ML: 0.259 / TLS residual ADP flag: LIKELY RESIDUAL
Isotropic thermal model: Isotropic with TLS (5 TLS groups per monomer)
Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 1.551 / ESU R Free: 0.356 / Stereochemistry target values: MAXIMUM LIKELIHOOD
RfactorNum. reflection% reflectionSelection details
Rfree0.25317 1250 5.1 %RANDOM
Rwork0.19151 ---
all0.19457 23492 --
obs0.19457 23335 99.33 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 63.549 Å2
Baniso -1Baniso -2Baniso -3
1-0.19 Å20.09 Å20 Å2
2--0.19 Å20 Å2
3----0.28 Å2
Refinement stepCycle: LAST / Resolution: 2.8→37.87 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5552 0 20 86 5658
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0130.0225673
X-RAY DIFFRACTIONr_angle_refined_deg1.3281.9527640
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.9045682
X-RAY DIFFRACTIONr_dihedral_angle_2_deg41.12124.236288
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.3151064
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.4621540
X-RAY DIFFRACTIONr_chiral_restr0.0930.2848
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.024250
X-RAY DIFFRACTIONr_nbd_refined0.230.22749
X-RAY DIFFRACTIONr_nbtor_refined0.3070.23953
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1360.2165
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2320.257
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1740.210
X-RAY DIFFRACTIONr_mcbond_it0.531.53493
X-RAY DIFFRACTIONr_mcangle_it0.93525516
X-RAY DIFFRACTIONr_scbond_it1.2932382
X-RAY DIFFRACTIONr_scangle_it2.1684.52124
Refine LS restraints NCS

Dom-ID: 1 / Auth asym-ID: A / Ens-ID: 1 / Refine-ID: X-RAY DIFFRACTION

NumberTypeRms dev position (Å)Weight position
1368tight positional0.080.05
1408medium positional0.540.5
1368tight thermal0.080.5
1408medium thermal0.522
LS refinement shellResolution: 2.8→2.872 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.318 87 -
Rwork0.259 1677 -
obs--97.78 %
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)
110.93943.6132-3.467518.2741-3.30110.87570.5131.97081.794-1.672-1.0588-0.2408-0.3058-0.63230.5459-0.3491-0.0620.15720.10760.64050.1482-52.458863.4575-37.9151
24.8256-0.40960.4176.1376-3.15162.92330.06580.29940.5970.14130.01360.0499-0.02090.0874-0.0794-0.224-0.04160.0439-0.1009-0.017-0.0611-58.019849.6433-23.9362
33.1186-0.28733.0620.8203-0.27493.68030.12930.0295-0.30120.02480.0520.0330.26040.2871-0.1813-0.11050.00810.0209-0.0696-0.0423-0.176-44.459631.90810.0893
45.0128-1.0688-3.17466.6317-1.140111.09950.1354-0.39720.35060.7801-0.089-0.2792-0.92551.1682-0.0463-0.2169-0.1271-0.13730.089-0.0376-0.3069-25.399538.114718.2444
53.6402-2.9848-1.74283.61175.328313.89240.2282-0.53541.36570.8510.0309-1.4369-1.67411.3531-0.2591-0.0514-0.3641-0.01910.1274-0.0650.0766-18.660247.873220.4629
612.5897-7.4344-2.94148.3519-0.61286.7334-1.2167-2.2027-1.9271.18341.1061.77930.2442-0.49880.1107-0.20270.02360.29430.03680.19140.0497-64.101350.813414.5118
77.7387-4.1364-3.66263.4192.30153.55350.16740.02680.5697-0.32260.0387-0.3146-0.0901-0.0532-0.2061-0.162-0.0859-0.0036-0.1304-0.0935-0.0776-50.842257.27110.292
81.6817-0.0305-0.93732.42951.95455.38930.1982-0.11410.3975-0.11240.2732-0.26380.29320.4153-0.4713-0.15240.0156-0.0092-0.073-0.0235-0.066-32.761644.3802-23.9243
98.06591.4906-2.10249.6327-4.622810.2888-0.02750.5016-0.1989-0.44760.18960.36861.0763-0.5987-0.16210.276-0.1081-0.0826-0.2154-0.1087-0.3902-38.397924.9857-41.8074
103.9539-0.21863.22627.7667-2.15373.13560.26840.8103-1.4408-0.5760.71951.10210.7291-0.4047-0.98790.2997-0.3371-0.249-0.14990.20460.0923-47.899917.8112-43.9243
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A706 - 730
2X-RAY DIFFRACTION2A731 - 828
3X-RAY DIFFRACTION3A831 - 968
4X-RAY DIFFRACTION4A969 - 1015
5X-RAY DIFFRACTION5A1016 - 1049
6X-RAY DIFFRACTION6B706 - 730
7X-RAY DIFFRACTION7B731 - 828
8X-RAY DIFFRACTION8B831 - 968
9X-RAY DIFFRACTION9B969 - 1015
10X-RAY DIFFRACTION10B1016 - 1049

+
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