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- PDB-8ftx: FlgN-FliJ fusion complex -

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Basic information

Entry
Database: PDB / ID: 8ftx
TitleFlgN-FliJ fusion complex
ComponentsFlagella biosynthesis chaperone FlgN, Flagellar FliJ protein fusion
KeywordsCHAPERONE / Chaperone-client complex
Function / homology
Function and homology information


bacterial-type flagellum organization / bacterial-type flagellum / bacterial-type flagellum assembly / cytoskeletal motor activity / bacterial-type flagellum-dependent cell motility / chemotaxis / protein transport / plasma membrane
Similarity search - Function
Flagellar export FliJ / Flagellar FliJ, proteobacteria / Flagellar FliJ protein / FlgN-like protein / FlgN-like superfamily / FlgN protein
Similarity search - Domain/homology
Flagellar FliJ protein / Flagella biosynthesis chaperone FlgN
Similarity search - Component
Biological speciesSalmonella enterica subsp. enterica serovar Typhimurium (bacteria)
MethodSOLUTION NMR / molecular dynamics
AuthorsRossi, P. / Kalodimos, C.G.
Funding support United States, Belgium, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI094623 United States
Research Foundation - Flanders (FWO)T3RecS G002516N Belgium
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

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Assembly

Deposited unit
A: Flagella biosynthesis chaperone FlgN, Flagellar FliJ protein fusion


Theoretical massNumber of molelcules
Total (without water)24,1171
Polymers24,1171
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 Flagella biosynthesis chaperone FlgN, Flagellar FliJ protein fusion / Flagella synthesis protein FlgN / Flagellar biosynthesis protein FlgN / Putative FlgK/FlgL export chaperone


Mass: 24116.904 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Salmonella enterica subsp. enterica serovar Typhimurium (bacteria)
Gene: flgN, fliJ / Production host: Escherichia coli (E. coli) / References: UniProt: A0A5K1US31, 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-13C HSQC
121isotropic12D 1H-15N HSQC
142isotropic22D 1H-15N HSQC
131isotropic13D HN(CA)CB
1141isotropic13D HN(COCA)CB
1131isotropic13D HNCO
1121isotropic13D 1H-15N NOESY
1112isotropic23D 1H-13C NOESY
1102isotropic23D 1H-13C NOESY aromatic
192isotropic23D 1H-15N NOESY
182isotropic23D CCH NOESY

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Sample preparation

Details
TypeSolution-IDContentsLabelSolvent systemDetails
solution1300 uM [U-13C; U-15N; U-2H] FlgN_1-113_FliJ_1-54_fusion, 20 mM potassium phosphate, 100 mM potassium chloride, 0.05 % sodium azide, 5 mM beta-mercaptoethanol, 95% H2O/5% D2Otriple95% H2O/5% D2O
solution2300 uM 15N_1H,13C_ILVMAT_CH3_U1H,13C_Tyr_Phe FlgN_1-113_FliJ_1-54_fusion, 20 mM potassium phosphate, 100 mM potassium chloride, 0.05 % sodium azide, 5 mM beta-mercaptoethanol, 95% H2O/5% D2ON_methyl_aro95% H2O/5% D2O15N_1H,13C_ILVMAT_CH3_U1H,13C_Tyr_Phe
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
300 uMFlgN_1-113_FliJ_1-54_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
300 uMFlgN_1-113_FliJ_1-54_fusion15N_1H,13C_ILVMAT_CH3_U1H,13C_Tyr_Phe2
20 mMpotassium phosphatenatural abundance2
100 mMpotassium chloridenatural abundance2
0.05 %sodium azidenatural abundance2
5 mMbeta-mercaptoethanolnatural abundance2
Sample conditionsIonic strength: 120 mM / Label: conditions_1 / pH: 7.0 / Pressure: 1 atm / Temperature: 298 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
NameDeveloperClassification
CNSBrunger, Adams, Clore, Gros, Nilges and Readrefinement
CYANAGuntert, Mumenthaler and Wuthrichstructure calculation
PINEBahrami, Markley, Assadi, and Eghbalniachemical shift assignment
SparkyGoddardpeak picking
TALOSCornilescu, Delaglio and Baxgeometry optimization
TopSpinBruker Biospincollection
PdbStattejero and montelioneprocessing
NMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxprocessing
RefinementMethod: molecular dynamics / Software ordinal: 1 / Details: MD in explicit water
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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