[English] 日本語
Yorodumi
- PDB-6nzl: Solution structure of POS-1, a CCCH-type Tandem Zinc Finger prote... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6nzl
TitleSolution structure of POS-1, a CCCH-type Tandem Zinc Finger protein from C. elegans
ComponentsCytoplasmic zinc-finger protein
KeywordsRNA BINDING PROTEIN / CCCH-type Tandem Zinc Finger protein
Function / homology
Function and homology information


Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA / Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA / embryonic pattern specification / embryo development ending in birth or egg hatching / P granule / cell fate specification / poly(U) RNA binding / mRNA 3'-UTR binding / transcription corepressor activity / regulation of translation ...Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA / Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA / embryonic pattern specification / embryo development ending in birth or egg hatching / P granule / cell fate specification / poly(U) RNA binding / mRNA 3'-UTR binding / transcription corepressor activity / regulation of translation / single-stranded RNA binding / negative regulation of transcription by RNA polymerase II / metal ion binding / cytosol / cytoplasm
Similarity search - Function
RNA-binding protein ZFP36-like / Zinc finger C-x8-C-x5-C-x3-H type (and similar) / Zinc finger, CCCH-type superfamily / zinc finger / Zinc finger, CCCH-type / Zinc finger C3H1-type profile.
Similarity search - Domain/homology
RNA-binding protein pos-1
Similarity search - Component
Biological speciesCaenorhabditis elegans (invertebrata)
MethodSOLUTION NMR / simulated annealing
AuthorsErtekin, A. / Massi, F.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01 GM117008 United States
CitationJournal: To Be Published
Title: Solution structure of POS-1, a CCCH-type Tandem Zinc Finger protein from C. elegans
Authors: Ertekin, A. / Massi, F.
History
DepositionFeb 14, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 14, 2020Provider: repository / Type: Initial release
Revision 1.1Jun 14, 2023Group: Database references / Other / Category: database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data
Revision 1.2May 15, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Cytoplasmic zinc-finger protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)9,0063
Polymers8,8751
Non-polymers1312
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 100target function
RepresentativeModel #1target function

-
Components

#1: Protein Cytoplasmic zinc-finger protein / POsterior Segregation


Mass: 8875.201 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Caenorhabditis elegans (invertebrata) / Gene: pos-1, CELE_F52E1.1, F52E1.1 / Plasmid: pet21a / Details (production host): N-terminal (6xHis)-Sumo tag / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: G5EF15
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
Has ligand of interestN

-
Experimental details

-
Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDSample stateSpectrometer-IDType
111isotropic22D 1H-15N HSQC
121isotropic22D 1H-13C HSQC
131isotropic22D 1H-13C HSQC aliphatic
141isotropic22D 1H-13C HSQC aromatic
151isotropic23D CBCA(CO)NH
161isotropic23D (H)CCH-TOCSY
171isotropic23D HBHA(CO)NH
181isotropic23D (H)CCH-COSY
191isotropic23D (H)CCH-TOCSY
1101isotropic23D HN(CA)CO
1111isotropic23D HNCA
1121isotropic23D HN(CA)CB
1131isotropic23D HNCO
1141isotropic23D HN(CO)CA
1151isotropic13D 1H-15N NOESY
1161isotropic13D 1H-13C NOESY
1171isotropic1(HB)CB(CGCDCE)HE
1181isotropic1(HB)CB(CGCD)HD

-
Sample preparation

DetailsType: solution
Contents: 0.4 mM [U-100% 13C; U-100% 15N] POS-1, 50 mM Tris-HCl pH 6.3, 100 mM potassium chloride, 100 uM Zinc Acetate, 1 mM DTT, 10 mM DSS, 92% H2O/8% D2O
Label: 13C15N / Solvent system: 92% H2O/8% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
0.4 mMPOS-1[U-100% 13C; U-100% 15N]1
50 mMTris-HCl pH 6.3natural abundance1
100 mMpotassium chloridenatural abundance1
100 uMZinc Acetatenatural abundance1
1 mMDTTnatural abundance1
10 mMDSSnatural abundance1
Sample conditionsIonic strength: 100 mM / Label: sample_1 / pH: 6.3 / Pressure: 1 atm / Temperature: 293 K

-
NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian Agilent VNMRSVarianAgilent VNMRS8001
Varian INOVAVarianINOVA6002

-
Processing

NMR software
NameDeveloperClassification
CNSBrunger A. T. et.al.refinement
CYANAGuntert, Mumenthaler and Wuthrichstructure calculation
PINEBahrami, Markley, Assadi, and Eghbalniachemical shift assignment
SparkyGoddardpeak picking
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: target function
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20

+
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