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Structure paper

TitleStructural basis of unisite catalysis of thermophilic FoF1-ATPase
Journal, issue, pagesTo Be Published
Publish dateApr 19, 2022 (structure data deposition date)
AuthorsNakano A / Yokoyama K / Kishikawa J / Nakanishi A / Mitsuoka K
External linksSearch PubMed
MethodsEM (single particle)
Resolution2.6 - 4.5 Å
Structure data

33251

7xkh

EMDB-33251, PDB-7xkh:
Nucleotide-depleted F1 domain of FoF1-ATPase from Bacillus PS3, state1
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-33252: Nucleotide-depleted F1 domain of FoF1-ATPase from Bacillus PS3, , state2
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-33253: Nucleotide-depleted FoF1-ATPase from Bacillus PS3, state3
Method: EM (single particle) / Resolution: 3.7 Å

33258

7xko

EMDB-33258, PDB-7xko:
F1 domain of epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state1,nucleotide depeleted
Method: EM (single particle) / Resolution: 3.4 Å

33259

7xkp

EMDB-33259, PDB-7xkp:
F1 domain of epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state1,unisite condition
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-33260: F1 domain of epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state1,unisite condition
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-33261: F1 domain of epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state2,nucleotide depleted
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-33262: F1 domain of epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state2,unisite condition
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-33263: F1 domain of epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state3,unisite condition
Method: EM (single particle) / Resolution: 3.8 Å

33264

7xkq

EMDB-33264, PDB-7xkq:
F1 domain of FoF1-ATPase with the down form of epsilon subunit from Bacillus PS3
Method: EM (single particle) / Resolution: 3.3 Å

33265

7xkr

EMDB-33265, PDB-7xkr:
F1 domain of FoF1-ATPase with the up form of epsilon subunit from Bacillus PS3
Method: EM (single particle) / Resolution: 2.6 Å

EMDB-33266: epsilon-inhibited FoF1-ATPase from Bacillus PS3 at saturated ATP-gamma-S condition, state1
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-33267: epsilon-inhibited FoF1-ATPase from Bacillus PS3 at saturated ATP-gamma-S condition, state2
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-33268: epsilon-inhibited FoF1-ATPase from Bacillus PS3 at saturated ATP-gamma-S condition, state3
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-33269: F1 domain of epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state2',nucleotide depleted
Method: EM (single particle) / Resolution: 4.5 Å

EMDB-33277: epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state1,nucleotide depleted
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-33278: epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state1,unisite condition
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-33279: epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state1',unisite condition
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-33280: epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state2,nucleotide depleted
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-33281: epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state2',nucleotide depleted
Method: EM (single particle) / Resolution: 4.5 Å

EMDB-33282: epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state2,unisite condition
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-33283: epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state3,unisite condition
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-34769: FoF1-ATPase from Bacillus PS3,100 degrees,state2,highATP
Method: EM (single particle) / Resolution: 4.1 Å

Chemicals

ChemComp-PI:
HYDROGENPHOSPHATE ION

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

Source
  • bacillus sp. ps3 (bacteria)
KeywordsMOTOR PROTEIN / ATP synthase F1 ATPase FoF1

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