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- PDB-1l6t: STRUCTURE OF ALA24/ASP61 TO ASP24/ASN61 SUBSTITUTED SUBUNIT C OF ... -

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Basic information

Entry
Database: PDB / ID: 1l6t
TitleSTRUCTURE OF ALA24/ASP61 TO ASP24/ASN61 SUBSTITUTED SUBUNIT C OF ESCHERICHIA COLI ATP SYNTHASE
ComponentsATP SYNTHASE C CHAIN
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. / Abildgaard, F. / Markley, J.L. / Fillingame, R.H.
CitationJournal: Biochemistry / Year: 2002
Title: Structure of Ala24/Asp61 --> Asp24/Asn61 substituted subunit c of Escherichia coli ATP synthase: implications for the mechanism of proton transport and rotary movement in the F0 complex.
Authors: Dmitriev, O.Y. / Abildgaard, F. / Markley, J.L. / Fillingame, R.H.
History
DepositionMar 13, 2002Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 24, 2002Provider: repository / Type: Initial release
Revision 1.1Apr 28, 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
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: ATP SYNTHASE C CHAIN


Theoretical massNumber of molelcules
Total (without water)8,3021
Polymers8,3021
Non-polymers00
Water00
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 C CHAIN / SUBUNIT C / Lipid-binding protein


Mass: 8302.090 Da / Num. of mol.: 1 / Mutation: A24D, D61N
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: uncE / Plasmid: pBR322 derivative / Production host: Escherichia coli (E. coli) / Strain (production host): JH618 / References: UniProt: P68699, EC: 3.6.3.34

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111HSQC
121HNCA
131CBCA(CO)NH
141HCACO
151HN(CO)CACB
161(H)CCH-TOCSY
171HC(CO)NH
1813D 13C-separated NOESY
1913D 15N-separated NOESY
11014D 13C/15N-separated NOESY

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Sample preparation

DetailsContents: 2.0 MM SUBUNIT C, 50 MM NACL, PH 5.0 / Solvent system: CDCl3:CD3OH:H20=4:4:1
Sample conditionsIonic strength: 50 mM NACL / pH: 5 / Pressure: ATMOSPHERIC atm / Temperature: 300.00 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 500 MHz

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Processing

NMR software
NameVersionDeveloperClassification
DYANA1.5P.GUENTERT, C.MUMENTHALER, K.WUETHRICHrefinement
DYANA1.5P.GUENTERT, C.MUMENTHALER, K.WUETHRICHstructure solution
XwinNMR2collection
Felix95processing
CHIFIT2R.A.Chylla, B.F.Volkman, J.L. Markleydata analysis
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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