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- PDB-2jty: Self-complemented variant of FimA, the main subunit of type 1 pilus -

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Basic information

Entry
Database: PDB / ID: 2jty
TitleSelf-complemented variant of FimA, the main subunit of type 1 pilus
ComponentsType-1 fimbrial protein, A chain
KeywordsSTRUCTURAL PROTEIN / PROTEIN/PILI/FIM / Cell projection / Fimbrium / chimera / CHAPERONE
Function / homology
Function and homology information


cell adhesion involved in single-species biofilm formation / pilus / cell adhesion / identical protein binding
Similarity search - Function
Fimbrial-type adhesion domain / Fimbrial-type adhesion domain / Fimbrial protein / Fimbrial-type adhesion domain superfamily / Adhesion domain superfamily / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Type-1 fimbrial protein, A chain
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR / torsion angle dynamics, molecular dynamics
AuthorsErilov, D. / Wider, G. / Glockshuber, R. / Puorger, C. / Vetsch, M.
CitationJournal: J.Mol.Biol. / Year: 2011
Title: Structure, Folding and Stability of FimA, the Main Structural Subunit of Type 1 Pili from Uropathogenic Escherichia coli Strains.
Authors: Puorger, C. / Vetsch, M. / Wider, G. / Glockshuber, R.
History
DepositionAug 9, 2007Deposition site: BMRB / Processing site: RCSB
Revision 1.0Aug 12, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Aug 17, 2011Group: Database references
Revision 1.3Sep 21, 2011Group: Database references
Revision 1.4Feb 19, 2020Group: Data collection / Database references / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_nmr_spectrometer
Item: _pdbx_database_status.status_code_cs / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model
Revision 1.5Jun 14, 2023Group: Database references / Other / Category: database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Type-1 fimbrial protein, A chain


Theoretical massNumber of molelcules
Total (without water)18,0341
Polymers18,0341
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)20 / 100target function
RepresentativeModel #1fewest violations

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Components

#1: Protein Type-1 fimbrial protein, A chain / Type-1A pilin


Mass: 18033.596 Da / Num. of mol.: 1
Fragment: Fusion protein of Type-1 fimbrial protein and type-1 fimbrial protein
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: fimA, pilA / Production host: Escherichia coli (E. coli) / References: UniProt: P04128
Sequence detailsTHE AUTHORS STATE THAT THIS PROTEIN IS DESIGNED TO MIMIC THE STATE OF FIMA SUBUNIT IN A CHAIN. THIS ...THE AUTHORS STATE THAT THIS PROTEIN IS DESIGNED TO MIMIC THE STATE OF FIMA SUBUNIT IN A CHAIN. THIS PROTEIN (FIMA) POLYMERIZES INTO A CHAIN IN E.COLI VIA A DOMAIN SWAPPING MECHANISM. EACH SUBUNIT DONATES ITS N-TERMINAL RESIDUES TO THE PRECEDING SUBUNIT TO COMPLEMENT ITS FOLD, WHICH OTHERWISE LACKS ONE BETA-STRAND.

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-15N HSQC
1212D 1H-13C HSQC
1313D HNCO
1413D HNCA
1513D HN(CA)CB
1613D HN(CO)CA
1713D 1H-15N NOESY
1813D 1H-13C NOESY
1913D 1H-15N TOCSY
11013D (H)CCH-TOCSY
1111CBHD
11213D 1H-13C NOESY aro
11312D 1H-13C HSQC aro

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Sample preparation

DetailsContents: 1.7 mM [U-98% 13C; U-98% 15N] FimA, 50 M H2O, 5 M D2O, 95% H2O/5% D2O
Solvent system: 95% H2O/5% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
1.7 mMFimA[U-98% 13C; U-98% 15N]1
50 MH2O1
5 MD2O1
Sample conditionsIonic strength: 18 / pH: 7.0 / Pressure: ambient / Temperature: 298 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AvanceBrukerAVANCE9001
Bruker DRXBrukerDRX7502

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Processing

NMR software
NameDeveloperClassification
CYANAGuntertstructure solution
OPALrefinement
RefinementMethod: torsion angle dynamics, molecular dynamics / Software ordinal: 1
Details: torsion angle dynamics using DYANA and molecular dynamics using Opal
NMR representativeSelection criteria: fewest violations
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20

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