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- PDB-1c99: ASP61 DEPROTONATED FORM OF SUBUNIT C OF THE F1FO ATP SYNTHASE OF ... -

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Basic information

Entry
Database: PDB / ID: 1c99
TitleASP61 DEPROTONATED FORM OF SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI
ComponentsPROTEOLIPID F1FO OF ATP SYNTHASE
KeywordsPROTON TRANSPORT / HYDROLASE / PROTEOLIPID F1FO / ATP SYNTHASE / PROTON TRANSLOCATION
Function / homology
Function and homology information


proton motive force-driven plasma membrane ATP synthesis / proton motive force-driven ATP synthesis / proton-transporting two-sector ATPase complex, proton-transporting domain / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase complex / 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
AuthorsRastogi, V.K. / Girvin, M.E.
Citation
Journal: Nature / Year: 1999
Title: Structural changes linked to proton translocation by subunit c of the ATP synthase.
Authors: Rastogi, V.K. / Girvin, M.E.
#1: Journal: J.Biomol.Nmr / Year: 1999
Title: 1H, 13C, and 15N assignments and secondary structure of the high pH form of subunit c of the F1F0 ATP synthase.
Authors: Rastogi, V.K. / Girvin, M.E.
#2: 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.
History
DepositionApr 30, 1999Deposition site: BNL / Processing site: RCSB
Revision 1.0Nov 19, 1999Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 27, 2019Group: Database references / Derived calculations
Category: citation / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _citation.journal_abbrev / _citation.page_last ..._citation.journal_abbrev / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.4Dec 27, 2023Group: 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

Structure viewerMolecule:
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Assembly

Deposited unit
A: PROTEOLIPID F1FO OF ATP SYNTHASE


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_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)9 / 20LEAST RESTRAINT VIOLATION
RepresentativeModel #9

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Components

#1: Protein PROTEOLIPID F1FO OF ATP SYNTHASE / E.C.3.6.1.34 / PROTEOLIPID / DCCD-BINDING PROTEIN


Mass: 8259.064 Da / Num. of mol.: 1 / Fragment: subunit c
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
151HNHA
161HN(CO)CA
171HN(CA)CB
181H(CCO)NH
191C(CO)NH
1101HCACO
1111(H)CCH-COSY
NMR detailsText: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED SUBUNIT C

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Sample preparation

Sample conditionspH: 8 / Temperature: 300 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker DRX600 / Manufacturer: Bruker / Model: DRX600 / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.854BRUNGERrefinement
CNS0.3BRUNGER et al.refinement
NMRPipeDelaglio, F. et al.data analysis
DYANAGuntert, P. et al.structure solution
RefinementMethod: torsion angle dynamics / Software ordinal: 1
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 20 / Conformers submitted total number: 9

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