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- PDB-8ftw: FliT-FliJ fusion complex -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 8ftw
TitleFliT-FliJ fusion complex
ComponentsFlagellar FliT protein, Flagellar FliJ protein fusion
KeywordsCHAPERONE / Chaperone-client complex
Function / homology
Function and homology information


negative regulation of bacterial-type flagellum assembly / bacterial-type flagellum organization / bacterial-type flagellum / cytoskeletal motor activity / bacterial-type flagellum-dependent cell motility / chemotaxis / protein transport / protein folding / plasma membrane / cytosol
Similarity search - Function
Flagellar export FliJ / Flagellar FliJ, proteobacteria / Flagellar FliJ protein / Flagellar protein FliT / Flagellar protein FliT
Similarity search - Domain/homology
Flagellar protein FliT / Flagellar FliJ protein
Similarity search - Component
Biological speciesSalmonella enterica subsp. enterica serovar Typhimurium (bacteria)
MethodSOLUTION NMR / molecular dynamics
AuthorsRossi, P. / Kalodimos, C.G.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI094623 United States
CitationJournal: J.Mol.Biol. / Year: 2023
Title: Chaperone Recycling in Late-Stage Flagellar Assembly.
Authors: Rossi, P. / Xing, Q. / Bini, E. / Portaliou, A.G. / Clay, M.C. / Warren, E.M. / Khanra, N.K. / Economou, A. / Kalodimos, C.G.
History
DepositionJan 13, 2023Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 5, 2023Provider: repository / Type: Initial release
Revision 1.1Nov 1, 2023Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / citation / Item: _citation.journal_volume

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Flagellar FliT protein, Flagellar FliJ protein fusion


Theoretical massNumber of molelcules
Total (without water)18,8271
Polymers18,8271
Non-polymers00
Water0
1


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

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Components

#1: Protein Flagellar FliT protein, Flagellar FliJ protein fusion


Mass: 18827.361 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Salmonella enterica subsp. enterica serovar Typhimurium (bacteria)
Gene: fliT, fliJ / Production host: Escherichia coli (E. coli) / References: UniProt: A0A0F7J9R1, UniProt: A0A5K1UBM0

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDSample stateSpectrometer-IDType
112isotropic22D 1H-15N HSQC
122isotropic22D 1H-13C HSQC
131isotropic13D HN(CA)CB
141isotropic13D HNCO
151isotropic13D HN(COCA)CB
1172isotropic23D 1H-13C NOESY
1162isotropic23D 1H-13C NOESY aromatic
1152isotropic23D 1H-15N NOESY
1141isotropic12D 1H-15N HSQC
1131isotropic13D 1H-15N NOESY

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Sample preparation

Details
TypeSolution-IDContentsDetailsLabelSolvent system
solution1400 uM [U-13C; U-15N; U-2H] FliT_1-95-FliJ_51-101_fusion, 20 mM potassium phosphate, 100 mM potassium chloride, 0.05 % sodium azide, 5 mM beta-mercaptoethanol, 95% H2O/5% D2Otriple labeledtriple95% H2O/5% D2O
solution2400 uM [U-100% 15N], 100% 13C-CH3_ILVMAT, 100%-1H,13C-Phe,Tyr FliT_1-95-FliJ_51-101_fusion, 20 mM potassium phosphate, 100 mM potassium chloride, 0.05 % sodium azide, 5 mM beta-mercaptoethanol, 95% H2O/5% D2O15N_ILVMAT_methyl_FY_aromaticN_methyl_aro95% H2O/5% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
400 uMFliT_1-95-FliJ_51-101_fusion[U-13C; U-15N; U-2H]1
20 mMpotassium phosphatenatural abundance1
100 mMpotassium chloridenatural abundance1
0.05 %sodium azidenatural abundance1
5 mMbeta-mercaptoethanolnatural abundance1
400 uMFliT_1-95-FliJ_51-101_fusion[U-100% 15N], 100% 13C-CH3_ILVMAT, 100%-1H,13C-Phe,Tyr2
20 mMpotassium phosphatenatural abundance2
100 mMpotassium chloridenatural abundance2
0.05 %sodium azidenatural abundance2
5 mMbeta-mercaptoethanolnatural abundance2
Sample conditionsIonic strength: 200 mM / Label: conditions_1 / pH: 7.0 / Pressure: 1 atm / Temperature: 25 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AVANCEBrukerAVANCE7001
Bruker AVANCEBrukerAVANCE8502

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Processing

NMR software
NameVersionDeveloperClassification
CNSBrunger, Adams, Clore, Gros, Nilges and Readrefinement
TopSpinBruker Biospincollection
NMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxprocessing
TALOSCornilescu, Delaglio and Baxgeometry optimization
PdbStattejero & montelioneprocessing
CYANA3.98Guntert, Mumenthaler and Wuthrichstructure calculation
PINEBahrami, Markley, Assadi, and Eghbalniachemical shift assignment
SparkyGoddardpeak picking
RefinementMethod: molecular dynamics / Software ordinal: 1 / Details: MD in explicit H2O
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20

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