|Entry||Database: EMDB / ID: EMD-12378|
|Title||Mycobacterium smegmatis ATP synthase F1 state 1a|
|Sample||Mycobacterium smegmatis ATP synthase|
|Function / homology|
Function and homology information
plasma membrane ATP synthesis coupled proton transport / proton-transporting ATP synthase complex, catalytic core F(1) / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / ATP binding / plasma membrane
Similarity search - Function
ATP synthase gamma subunit signature. / ATP synthase, F1 complex, beta subunit / ATP synthase, F1 complex, gamma subunit conserved site / ATP synthase / ATP synthase, F1 complex, gamma subunit / ATP synthase, F1 complex, gamma subunit superfamily / ATP synthase alpha/beta chain, C terminal domain / ATP synthase, alpha subunit, C-terminal domain superfamily / ATP synthase, alpha subunit, C-terminal / ATP synthase, F1 complex, alpha subunit nucleotide-binding domain ...ATP synthase gamma subunit signature. / ATP synthase, F1 complex, beta subunit / ATP synthase, F1 complex, gamma subunit conserved site / ATP synthase / ATP synthase, F1 complex, gamma subunit / ATP synthase, F1 complex, gamma subunit superfamily / ATP synthase alpha/beta chain, C terminal domain / ATP synthase, alpha subunit, C-terminal domain superfamily / ATP synthase, alpha subunit, C-terminal / ATP synthase, F1 complex, alpha subunit nucleotide-binding domain / ATP synthase, F1 complex, alpha subunit / ATPase, F1/V1 complex, beta/alpha subunit, C-terminal / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain superfamily / ATP synthase subunit alpha, N-terminal domain-like superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain / ATP synthase alpha/beta family, beta-barrel domain / ATPase, alpha/beta subunit, nucleotide-binding domain, active site / ATP synthase alpha and beta subunits signature. / ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain / ATP synthase alpha/beta family, nucleotide-binding domain / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ATP synthase subunit beta / ATP synthase gamma chain / ATP synthase subunit alpha
Similarity search - Component
|Biological species||Mycolicibacterium smegmatis MC2 155 (bacteria)|
|Method||single particle reconstruction / cryo EM / Resolution: 2.52 Å|
|Authors||Petri J / Montgomery MG / Spikes TE / Walker JE|
|Funding support|| United Kingdom, 2 items |
|Citation||Journal: Proc Natl Acad Sci U S A / Year: 2021|
Title: Structure of the ATP synthase from provides targets for treating tuberculosis.
Authors: Martin G Montgomery / Jessica Petri / Tobias E Spikes / John E Walker /
Abstract: The structure has been determined by electron cryomicroscopy of the adenosine triphosphate (ATP) synthase from This analysis confirms features in a prior description of the structure of the enzyme, ...The structure has been determined by electron cryomicroscopy of the adenosine triphosphate (ATP) synthase from This analysis confirms features in a prior description of the structure of the enzyme, but it also describes other highly significant attributes not recognized before that are crucial for understanding the mechanism and regulation of the mycobacterial enzyme. First, we resolved not only the three main states in the catalytic cycle described before but also eight substates that portray structural and mechanistic changes occurring during a 360° catalytic cycle. Second, a mechanism of auto-inhibition of ATP hydrolysis involves not only the engagement of the C-terminal region of an α-subunit in a loop in the γ-subunit, as proposed before, but also a "fail-safe" mechanism involving the b'-subunit in the peripheral stalk that enhances engagement. A third unreported characteristic is that the fused bδ-subunit contains a duplicated domain in its N-terminal region where the two copies of the domain participate in similar modes of attachment of the two of three N-terminal regions of the α-subunits. The auto-inhibitory plus the associated "fail-safe" mechanisms and the modes of attachment of the α-subunits provide targets for development of innovative antitubercular drugs. The structure also provides support for an observation made in the bovine ATP synthase that the transmembrane proton-motive force that provides the energy to drive the rotary mechanism is delivered directly and tangentially to the rotor via a Grotthuss water chain in a polar L-shaped tunnel.
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_12378.map.gz / Format: CCP4 / Size: 476.8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 0.83 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire Mycobacterium smegmatis ATP synthase
|Entire||Name: Mycobacterium smegmatis ATP synthase / Number of Components: 1|
-Component #1: protein, Mycobacterium smegmatis ATP synthase
|Protein||Name: Mycobacterium smegmatis ATP synthase / Recombinant expression: No|
|Source||Species: Mycolicibacterium smegmatis MC2 155 (bacteria)|
|Source (engineered)||Expression System: Mycolicibacterium smegmatis (bacteria) / Strain: mc2 4517|
|Specimen||Specimen State: Particle / Method: cryo EM|
|Sample solution||pH: 8|
|Vitrification||Cryogen Name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron Source: FIELD EMISSION GUN / Accelerating Voltage: 300 kV / Electron Dose: 59.86 e/Å2 / Illumination Mode: FLOOD BEAM|
|Lens||Imaging Mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
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