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- PDB-1a91: SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI; NMR, 10 S... -

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Basic information

Entry
Database: PDB / ID: 1a91
TitleSUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI; NMR, 10 STRUCTURES
ComponentsF1FO ATPASE SUBUNIT C
KeywordsMEMBRANE PROTEIN / HYDROGEN ION TRANSPORT
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 / torsion angle dynamics
AuthorsGirvin, M.E. / Rastogi, V.K. / Abildgaard, F. / Markley, J.L. / Fillingame, R.H.
Citation
Journal: Biochemistry / Year: 1998
Title: Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase.
Authors: Girvin, M.E. / Rastogi, V.K. / Abildgaard, F. / Markley, J.L. / Fillingame, R.H.
#1: Journal: Biochemistry / Year: 1995
Title: Determination of Local Protein Structure by Spin Label Difference 2D NMR: The Region Neighboring Asp61 of Subunit C of the F1F0 ATP Synthase
Authors: Girvin, M.E. / Fillingame, R.H.
History
DepositionApr 15, 1998Processing site: BNL
Revision 1.0Jul 1, 1998Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _pdbx_nmr_software.name
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
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Assembly

Deposited unit
A: F1FO ATPASE SUBUNIT C


Theoretical massNumber of molelcules
Total (without water)8,2591
Polymers8,2591
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 20LEAST RESTRAINT VIOLATION
Representative

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Components

#1: Protein F1FO ATPASE SUBUNIT C / PROTEOLIPID / DCCD-BINDING PROTEIN


Mass: 8259.064 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: ER / Cellular location: MEMBRANE / Gene: UNCE / Production host: Escherichia coli (E. coli) / Strain (production host): ER / 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
111HSQC
121TOCSY-HSQC
131NOESY-HSQC
141HNCO
151HNCA
161HN(CO)CA
171HN(CA)CB
181CBCA(CO)NH
191H (CCO)NH
1101C(CO)NH
1111HCACO
1121AND HNCA-J

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Sample preparation

Sample conditionspH: 5 / Temperature: 300 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DMX500BrukerDMX5005001
Bruker DRX600BrukerDRX6006002

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Processing

Software
NameClassification
DYANAmodel building
X-PLORmodel building
DYANArefinement
X-PLORrefinement
NMR software
NameDeveloperClassification
X-PLORBRUNGERrefinement
NMRPipestructure solution
DYANAstructure solution
X-PLORstructure solution
RefinementMethod: torsion angle dynamics / Software ordinal: 1
Details: SIMULATED ANNEALING, WITH NOE, TORSION ANGLE, AND HYDROGEN BOND NMR-DERIVED CONSTRAINTS. STARTING AT 750K AND COOLING TO 300K.
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 20 / Conformers submitted total number: 10

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