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- PDB-1ijp: Solution Structure of Ala20Pro/Pro64Ala substituted subunit c of ... -

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Basic information

Entry
Database: PDB / ID: 1ijp
TitleSolution Structure of Ala20Pro/Pro64Ala substituted subunit c of Escherichia coli ATP synthase
ComponentsATP Synthase
KeywordsHYDROLASE / transmembrane helix
Function / homology
Function and homology information


proton-transporting ATP synthase complex / proton motive force-driven plasma membrane ATP synthesis / proton-transporting ATP synthase complex, coupling factor F(o) / proton motive force-driven ATP synthesis / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / lipid binding / plasma membrane
Similarity search - Function
F1F0 ATP synthase subunit C / F1FO ATP Synthase / ATP synthase, F0 complex, subunit C, bacterial/chloroplast / ATP synthase, F0 complex, subunit C / F1F0 ATP synthase subunit C superfamily / ATP synthase, F0 complex, subunit C, DCCD-binding site / ATP synthase c subunit signature. / V-ATPase proteolipid subunit C-like domain / F/V-ATP synthase subunit C superfamily / ATP synthase subunit C ...F1F0 ATP synthase subunit C / F1FO ATP Synthase / ATP synthase, F0 complex, subunit C, bacterial/chloroplast / ATP synthase, F0 complex, subunit C / F1F0 ATP synthase subunit C superfamily / ATP synthase, F0 complex, subunit C, DCCD-binding site / ATP synthase c subunit signature. / V-ATPase proteolipid subunit C-like domain / F/V-ATP synthase subunit C superfamily / ATP synthase subunit C / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
ATP synthase subunit c
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR / simulated annealing, torsion angle dynamics
AuthorsDmitriev, O.Y. / Fillingame, R.H.
CitationJournal: J.Biol.Chem. / Year: 2001
Title: Structure of Ala(20) --> Pro/Pro(64) --> Ala substituted subunit c of Escherichia coli ATP synthase in which the essential proline is switched between transmembrane helices.
Authors: Dmitriev, O.Y. / Fillingame, R.H.
History
DepositionApr 27, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 27, 2002Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 27, 2021Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: ATP Synthase


Theoretical massNumber of molelcules
Total (without water)8,2591
Polymers8,2591
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 200target function
Representative

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Components

#1: Protein ATP Synthase /


Mass: 8259.064 Da / Num. of mol.: 1 / Fragment: subunit c / Mutation: A20P, P64A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: uncE / Plasmid: pBR322 / Production host: Escherichia coli (E. coli) / Strain (production host): JH613 / References: UniProt: P68699, EC: 3.6.1.34

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111DQF-COSY
1212D TOCSY
1313D 15N-separated TOCSY
1412D NOESY
1513D 15N-separated NOESY
161HNHA

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Sample preparation

DetailsContents: 2.2 mM subunit c, 50 mM NaCl, pH 5.0
Solvent system: CDCl3:CD3OD:D2O=4:4:1 or CDCl3:CD3OH:H2O=4:4:1
Sample conditionsIonic strength: 50 mM NaCl / pH: 5.0 / Pressure: atmospheric atm / Temperature: 300 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz

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Processing

NMR software
NameVersionClassification
XwinNMRcollection
Felix95data analysis
DYANA1.5structure solution
Discover3refinement
RefinementMethod: simulated annealing, torsion angle dynamics / Software ordinal: 1
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 200 / Conformers submitted total number: 10

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