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- PDB-2mn7: Solution structure of monomeric TatA of twin-arginine translocati... -

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Basic information

Entry
Database: PDB / ID: 2mn7
TitleSolution structure of monomeric TatA of twin-arginine translocation system from E. coli
ComponentsSec-independent protein translocase protein TatA
KeywordsTRANSPORT PROTEIN
Function / homology
Function and homology information


proton motive force dependent protein transmembrane transporter activity / TAT protein transport complex / protein transport by the Tat complex / intracellular protein transmembrane transport / protein transmembrane transporter activity / identical protein binding / plasma membrane / cytosol
Similarity search - Function
Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #3310 / Sec-independent protein translocase protein TatA/B/E / Sec-independent protein translocase protein TatA/E / mttA/Hcf106 family / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Sec-independent protein translocase protein TatA
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR / simulated annealing
Model detailslowest energy, model1
AuthorsZhang, Y. / Hu, Y. / Jin, C.
CitationJournal: Plos One / Year: 2014
Title: Structural basis for TatA oligomerization: an NMR study of Escherichia coli TatA dimeric structure
Authors: Zhang, Y. / Hu, Y. / Li, H. / Jin, C.
History
DepositionMar 31, 2014Deposition site: BMRB / Processing site: PDBJ
Revision 1.0Apr 15, 2015Provider: repository / Type: Initial release
Revision 1.1Jun 14, 2023Group: Data collection / Database references / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_nmr_spectrometer / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _struct_ref_seq_dif.details
Revision 1.2May 15, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

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Structure visualization

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Assembly

Deposited unit
A: Sec-independent protein translocase protein TatA


Theoretical massNumber of molelcules
Total (without water)10,7491
Polymers10,7491
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 100structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein Sec-independent protein translocase protein TatA


Mass: 10749.122 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: tatA, mttA1, yigT, b3836, JW3813 / Production host: Escherichia coli (E. coli) / References: UniProt: P69428

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 1H-13C NOESY
1212D 1H-15N HSQC
1312D 1H-13C HSQC
1413D 1H-15N NOESY
1513D 1H-13C NOESY aliphatic
1613D HNCO
1713D HNCA

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Sample preparation

DetailsContents: 1 mM [U-99% 13C; U-99% 15N] protein-1, 50 mM sodium phosphate-2, 200 mM DPC-3, 90% H2O/10% D2O
Solvent system: 90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
1 mMprotein-1[U-99% 13C; U-99% 15N]1
50 mMsodium phosphate-21
200 mMDPC-31
Sample conditionsIonic strength: 0.05 / pH: 7 / Pressure: ambient / Temperature: 308 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AvanceBrukerAVANCE8001
Bruker AvanceBrukerAVANCE7002
Bruker AvanceBrukerAVANCE6003

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Processing

NMR software
NameDeveloperClassification
NMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxprocessing
NMRViewJohnson, One Moon Scientificdata analysis
TopSpinBruker Biospincollection
X-PLOR NIHSchwieters, Kuszewski, Tjandra and Clorestructure solution
X-PLOR NIHSchwieters, Kuszewski, Tjandra and Clorerefinement
HADDOCKrefinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 20 / Representative conformer: 1

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