[English] 日本語
Yorodumi
- PDB-7nmb: cytoplasmic domain of Vibrio cholerae ToxR -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7nmb
Titlecytoplasmic domain of Vibrio cholerae ToxR
ComponentsCholera toxin transcriptional activator
KeywordsTRANSCRIPTION / DNA binding domain wHTH transcription factor
Function / homologyOmpR/PhoB-type DNA-binding domain / Transcriptional regulatory protein, C terminal / Transcriptional regulatory protein, C terminal / Signal transduction response regulator, C-terminal effector / phosphorelay signal transduction system / Winged helix-like DNA-binding domain superfamily / regulation of DNA-templated transcription / DNA binding / Cholera toxin transcriptional activator
Function and homology information
Biological speciesVibrio cholerae (bacteria)
MethodSOLUTION NMR / simulated annealing
AuthorsGubensaek, N. / Zangger, K. / Hartlmueller, C. / Madl, T.
Funding support Austria, 1items
OrganizationGrant numberCountry
Austrian Science FundW9 DK Austria
CitationJournal: J.Biol.Chem. / Year: 2021
Title: Structural and DNA-binding properties of the cytoplasmic domain of Vibrio cholerae transcription factor ToxR.
Authors: Gubensak, N. / Schrank, E. / Hartlmuller, C. / Gobl, C. / Falsone, F.S. / Becker, W. / Wagner, G.E. / Pulido, S. / Meyer, N.H. / Pavkov-Keller, T. / Madl, T. / Reidl, J. / Zangger, K.
History
DepositionFeb 23, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 20, 2021Provider: repository / Type: Initial release
Revision 1.1Nov 10, 2021Group: Data collection / Database references / Category: citation / pdbx_database_proc / Item: _citation.journal_volume / _citation.title

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Cholera toxin transcriptional activator


Theoretical massNumber of molelcules
Total (without water)16,6421
Polymers16,6421
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: homology
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area0 Å2
ΔGint0 kcal/mol
Surface area7310 Å2
MethodPISA
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)5 / 100000back calculated data agree with experimental NOESY spectrum
RepresentativeModel #1closest to the average

-
Components

#1: Protein Cholera toxin transcriptional activator


Mass: 16641.771 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Vibrio cholerae (bacteria) / Gene: toxR, ERS013165_01791 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A655QCS4

-
Experimental details

-
Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDSample stateSpectrometer-IDType
111isotropic12D 1H-15N HSQC
121isotropic12D 1H-13C HSQC
131isotropic13D HNCA
141isotropic13D HNCO
151isotropic13D HN(CO)CA
161isotropic13D (H)CCH-TOCSY
191isotropic13D HN(CA)CB
181isotropic13D HN(CA)CO
171isotropic13D 1H-13C NOESY aromatic
1111isotropic13D 1H-15N NOESY
1101isotropic13D 1H-13C NOESY
1131isotropic1H(CCO)NH
1121isotropic1H(CCO)NH

-
Sample preparation

DetailsType: solution
Contents: 400 uM [U-13C; U-15N] cToxR_1-134, 90% H2O/10% D2O
Label: 13C_15N_cToxR / Solvent system: 90% H2O/10% D2O
SampleConc.: 400 uM / Component: cToxR_1-134 / Isotopic labeling: [U-13C; U-15N]
Sample conditionsIonic strength: 100 mM / Label: conditions_1 / pH: 6.5 / Pressure: 1 bar / Temperature: 298 K

-
NMR measurement

NMR spectrometerType: Bruker AVANCE III / Manufacturer: Bruker / Model: AVANCE III / Field strength: 700 MHz

-
Processing

NMR software
NameDeveloperClassification
NMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxprocessing
CcpNmr AnalysisCCPNchemical shift assignment
CS-ROSETTAShen, Vernon, Baker and Baxstructure calculation
RefinementMethod: simulated annealing / Software ordinal: 3
NMR representativeSelection criteria: closest to the average
NMR ensembleConformer selection criteria: back calculated data agree with experimental NOESY spectrum
Conformers calculated total number: 100000 / Conformers submitted total number: 5

+
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