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- PDB-2lzr: TatA T22P -

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Basic information

Entry
Database: PDB / ID: 2lzr
TitleTatA T22P
ComponentsSec-independent protein translocase protein TatA
KeywordsPROTEIN TRANSPORT / MEMBRANE PROTEIN / TATA / DPC
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 / lipid binding / 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
AuthorsRodriguez, F.M. / Berks, B.C. / Schnell, J.R.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2013
Title: Structural model for the protein-translocating element of the twin-arginine transport system.
Authors: Rodriguez, F. / Rouse, S.L. / Tait, C.E. / Harmer, J. / De Riso, A. / Timmel, C.R. / Sansom, M.S. / Berks, B.C. / Schnell, J.R.
History
DepositionOct 8, 2012Deposition site: BMRB / Processing site: RCSB
Revision 1.0Mar 20, 2013Provider: repository / Type: Initial release
Revision 1.1Apr 24, 2013Group: Database references
Revision 1.2Jun 14, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / struct_conn / 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 / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Sec-independent protein translocase protein TatA


Theoretical massNumber of molelcules
Total (without water)6,0061
Polymers6,0061
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 200structures with the lowest energy
RepresentativeModel #1closest to the average

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Components

#1: Protein Sec-independent protein translocase protein TatA


Mass: 6006.097 Da / Num. of mol.: 1 / Mutation: T22P
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: b3836, JW3813, mttA1, tatA, yigT / Plasmid: pET24 TatAd40 T22P / 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
1123D HNCA
1223D HNCO
1313D 1H-15N NOESY
1413D 1H-15N TOCSY
1533D 1H-13C NOESY aliphatic
1633D 1H-13C NOESY aromatic
1723D HNCO

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Sample preparation

Details
Solution-IDContentsSolvent system
10.5 mM [U-100% 15N] Protein, 240 mM DPC, 95% H2O/5% D2O95% H2O/5% D2O
20.5 mM [U-100% 13C; U-100% 15N] Protein, 240 mM DPC, 95% H2O/5% D2O95% H2O/5% D2O
30.5 mM [U-100% 13C; U-100% 15N] Protein, 240 mM [U-100% 2H] DPC, 95% H2O/5% D2O95% H2O/5% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
0.5 mMProtein-1[U-100% 15N]1
240 mMDPC-21
0.5 mMProtein-3[U-100% 13C; U-100% 15N]2
240 mMDPC-42
0.5 mMProtein-5[U-100% 13C; U-100% 15N]3
240 mMDPC-6[U-100% 2H]3
Sample conditionsIonic strength: 0.05 / pH: 7.0 / Pressure: ambient / Temperature: 303 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Homebuilt OMEGAHome-builtOMEGA9501
Homebuilt OMEGAHome-builtOMEGA6002
Homebuilt OMEGAHome-builtOMEGA7503
Bruker AVIIBrukerAVII5004

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Processing

NMR software
NameDeveloperClassification
X-PLOR NIHSchwieters, Kuszewski, Tjandra and Clorestructure solution
X-PLOR NIHSchwieters, Kuszewski, Tjandra and Clorerefinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR constraintsNOE constraints total: 542
NMR representativeSelection criteria: closest to the average
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 200 / Conformers submitted total number: 10

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