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- PDB-1bsh: SOLUTION STRUCTURE OF THE EPSILON SUBUNIT OF THE F1-ATPSYNTHASE F... -

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Entry
Database: PDB / ID: 1bsh
TitleSOLUTION STRUCTURE OF THE EPSILON SUBUNIT OF THE F1-ATPSYNTHASE FROM ESCHERICHIA COLI AND ORIENTATION OF THE SUBUNIT RELATIVE TO THE BETA SUBUNITS OF THE COMPLEX
ComponentsPROTEIN (EPSILON SUBUNIT)
KeywordsHYDROLASE / ATPSYNTHASE / F1-ATPASE / EPSILON SUBUNIT / NMR SPECTROSCOPY
Function / homology
Function and homology information


proton motive force-driven plasma membrane ATP synthesis / proton motive force-driven ATP synthesis / proton-transporting ATP synthase complex / proton-transporting ATP synthase activity, rotational mechanism / ATP binding / plasma membrane
Similarity search - Function
ATP synthase delta/epsilon subunit, C-terminal domain / ATP Synthase; domain 1 / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase delta/epsilon subunit, C-terminal domain / ATP synthase, Delta/Epsilon chain, long alpha-helix domain / ATP synthase delta/epsilon subunit, C-terminal domain superfamily / ATP synthase, F1 complex, delta/epsilon subunit / ATP synthase, F1 complex, delta/epsilon subunit, N-terminal / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase, Delta/Epsilon chain, beta-sandwich domain ...ATP synthase delta/epsilon subunit, C-terminal domain / ATP Synthase; domain 1 / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase delta/epsilon subunit, C-terminal domain / ATP synthase, Delta/Epsilon chain, long alpha-helix domain / ATP synthase delta/epsilon subunit, C-terminal domain superfamily / ATP synthase, F1 complex, delta/epsilon subunit / ATP synthase, F1 complex, delta/epsilon subunit, N-terminal / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase, Delta/Epsilon chain, beta-sandwich domain / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Up-down Bundle / Sandwich / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
ATP synthase epsilon chain
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR / distance geometry
AuthorsWilkens, S. / Capaldi, R.A.
Citation
Journal: J.Biol.Chem. / Year: 1998
Title: Solution structure of the epsilon subunit of the F1-ATPase from Escherichia coli and interactions of this subunit with beta subunits in the complex.
Authors: Wilkens, S. / Capaldi, R.A.
#1: Journal: Nat.Struct.Biol. / Year: 1995
Title: Structural Features of the Epsilon Subunit of the Escherichia Coli ATP Synthase Determined by NMR Spectroscopy
Authors: Wilkens, S. / Dahlquist, F.W. / Mcintosh, L.P. / Donaldson, L.W. / Capaldi, R.A.
History
DepositionAug 27, 1998Deposition site: BNL / Processing site: RCSB
Revision 1.0Sep 2, 1998Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jul 7, 2021Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Experimental preparation / Refinement description
Category: pdbx_database_related / pdbx_nmr_details ...pdbx_database_related / pdbx_nmr_details / pdbx_nmr_ensemble / pdbx_nmr_exptl_sample_conditions / pdbx_nmr_refine / pdbx_nmr_software / pdbx_nmr_spectrometer / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _pdbx_database_related.content_type / _pdbx_database_related.details ..._pdbx_database_related.content_type / _pdbx_database_related.details / _pdbx_nmr_details.text / _pdbx_nmr_ensemble.conformer_selection_criteria / _pdbx_nmr_exptl_sample_conditions.pressure_units / _pdbx_nmr_refine.details / _pdbx_nmr_refine.method / _pdbx_nmr_software.authors / _pdbx_nmr_software.classification / _pdbx_nmr_software.version / _pdbx_nmr_spectrometer.manufacturer / _pdbx_nmr_spectrometer.model
Revision 1.4Apr 10, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

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Assembly

Deposited unit
A: PROTEIN (EPSILON SUBUNIT)


Theoretical massNumber of molelcules
Total (without water)14,9561
Polymers14,9561
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)30 / 30all calculated structures submitted
Representative

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Components

#1: Protein PROTEIN (EPSILON SUBUNIT) / EC 3.6.1.34 HYDROLASE


Mass: 14956.047 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: UNCC / Plasmid: PES2 / Gene (production host): UNCC / Production host: Escherichia coli (E. coli) / Strain (production host): K38, 594, DL39, 435 / References: UniProt: P0A6E6, 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
1113D NOESY-HSMQC
1213D TOCSY-HSMQC
1313D C(CO)NH
1413D H(CCO)NH
151SIMULTANEOUS 13C/ 15N RESOLVED NOESY
161VARIOUS 2D EXPERIMENTS
NMR detailsText: THE STRUCTURE OF THE E. COLI ATPASE EPSILON SUBUNIT WAS DETERMINED USING TRIPLE-RESONANCE NMR EXPERIMENTS WITH 15N AND 13C/15N LABELED PROTEIN.

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Sample preparation

Sample conditionsIonic strength: 0.03 / pH: 7.4 / Pressure: 10000 Pa / Temperature: 295 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
GE GNGEGN5001
Varian UNITYVarianUNITY5002

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.1BRUNGERrefinement
X-PLOR3.1BRUNGERstructure calculation
RefinementMethod: distance geometry / Software ordinal: 1 / Details: simulated annealing and molecular dynamics
NMR ensembleConformer selection criteria: all calculated structures submitted
Conformers calculated total number: 30 / Conformers submitted total number: 30

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