7Y5B
Cryo-EM structure of F-ATP synthase from Mycolicibacterium smegmatis (rotational state 1)
Summary for 7Y5B
| Entry DOI | 10.2210/pdb7y5b/pdb |
| EMDB information | 33615 |
| Descriptor | ATP synthase subunit alpha, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (12 entities in total) |
| Functional Keywords | complex, f-atp synthase, cryo-em, mycobacteria, hydrolase |
| Biological source | Mycolicibacterium smegmatis More |
| Total number of polymer chains | 20 |
| Total formula weight | 553804.10 |
| Authors | Saw, W.-G.,Wong, C.F.,Grueber, G. (deposition date: 2022-06-16, release date: 2022-11-23, Last modification date: 2024-07-03) |
| Primary citation | Wong, C.F.,Saw, W.G.,Basak, S.,Sano, M.,Ueno, H.,Kerk, H.W.,Litty, D.,Ragunathan, P.,Dick, T.,Muller, V.,Noji, H.,Gruber, G. Structural Elements Involved in ATP Hydrolysis Inhibition and ATP Synthesis of Tuberculosis and Nontuberculous Mycobacterial F-ATP Synthase Decipher New Targets for Inhibitors. Antimicrob.Agents Chemother., 66:e0105622-e0105622, 2022 Cited by PubMed Abstract: 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. PubMed: 36445139DOI: 10.1128/aac.01056-22 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.4 Å) |
Structure validation
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