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TitleStructural Elements Involved in ATP Hydrolysis Inhibition and ATP Synthesis of Tuberculosis and Nontuberculous Mycobacterial F-ATP Synthase Decipher New Targets for Inhibitors.
Journal, issue, pagesAntimicrob Agents Chemother, Vol. 66, Issue 12, Page e0105622, Year 2022
Publish dateDec 20, 2022
AuthorsChui Fann Wong / Wuan-Geok Saw / Sandip Basak / Mio Sano / Hiroshi Ueno / Hwee Wen Kerk / Dennis Litty / Priya Ragunathan / Thomas Dick / Volker Müller / Hiroyuki Noji / Gerhard Grüber /
PubMed AbstractThe FF-ATP synthase is required for the viability of tuberculosis (TB) and nontuberculous mycobacteria (NTM) and has been validated as a drug target. Here, we present the cryo-EM structures of the ...The FF-ATP synthase is required for the viability of tuberculosis (TB) and nontuberculous mycobacteria (NTM) and has been validated as a drug target. Here, we present the cryo-EM structures of the Mycobacterium smegmatis F-ATPase and the FF-ATP synthase with different nucleotide occupation within the catalytic sites and visualize critical elements for latent ATP hydrolysis and efficient ATP synthesis. Mutational studies reveal that the extended C-terminal domain (αCTD) of subunit α is the main element for the self-inhibition mechanism of ATP hydrolysis for TB and NTM bacteria. Rotational studies indicate that the transition between the inhibition state by the αCTD and the active state is a rapid process. We demonstrate that the unique mycobacterial γ-loop and subunit δ are critical elements required for ATP formation. The data underline that these mycobacterium-specific elements of α, γ, and δ are attractive targets, providing a platform for the discovery of species-specific inhibitors.
External linksAntimicrob Agents Chemother / PubMed:36445139 / PubMed Central
MethodsEM (single particle)
Resolution3.5 - 7.3 Å
Structure data

33614

7y5a

EMDB-33614, PDB-7y5a:
Cryo-EM structure of the Mycolicibacterium smegmatis F1-ATPase
Method: EM (single particle) / Resolution: 3.5 Å

33615

7y5b

EMDB-33615, PDB-7y5b:
Cryo-EM structure of F-ATP synthase from Mycolicibacterium smegmatis (rotational state 1)
Method: EM (single particle) / Resolution: 4.4 Å

33616

7y5c

EMDB-33616, PDB-7y5c:
Cryo-EM structure of F-ATP synthase from Mycolicibacterium smegmatis (rotational state 2)
Method: EM (single particle) / Resolution: 4.7 Å

33617

7y5d

EMDB-33617, PDB-7y5d:
Cryo-EM structure of F-ATP synthase from Mycolicibacterium smegmatis (rotational state 3) (backbone)
Method: EM (single particle) / Resolution: 7.3 Å

Chemicals

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

ChemComp-MG:
Unknown entry

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

Source
  • mycolicibacterium smegmatis (bacteria)
KeywordsHYDROLASE / Complex / F-ATP synthase / cryo-EM / mycobacteria

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