ATP synthase alpha/beta subunits

ATP synthase alpha/beta family, nucleotide-binding domain
ATP synthase alpha/beta family, nucleotide-binding domain
Identifiers
Symbol	ATP-synt_ab
Pfam	PF00006
InterPro	IPR000194
PROSITE	PDOC00137
SCOP2	1bmf / SCOPe / SUPFAM
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1jva A:273-746 1gpp A:283-482 1vde A:283-736 1um2 D:273-287 1lwt A:283-736 1dfa A:283-736 1lws A:283-736 1fx0 B:151-372 1kmh B:151-372 1e1i A:126-348 1e16 A:126-348 1e1r D:185-405 1bmf D:185-405 1nbm D:185-405 1cow F:185-405 1h8e E:185-405 1efr E:185-405 1h8h F:185-405 1w0k D:185-405 1e1q E:185-405 1w0j E:185-405 1e79 E:185-405 1sky E:137-351 1nvz A:129-349 1v0i A:147-357 2bn9 A:154-364

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1fx0 B:23-95 1kmh B:23-95 1nvz A:6-73 1sky E:6-80 1e1r D:63-129 1bmf D:63-129 1nbm D:63-129 1cow F:63-129 1h8e E:63-129 1efr E:63-129 1h8h F:63-129 1w0k D:63-129 1e1q E:63-129 1w0j E:63-129 1e79 E:63-129 1e16 A:4-70 1e1i A:4-70 1v0i A:26-91 2bn9 A:21-92

ATP synthase alpha/beta family, beta-barrel domain
ATP synthase alpha/beta family, beta-barrel domain
	Simplified model of FOF1-ATPase alias ATP synthase of E. coli. Subunits of the enzyme are labeled accordingly.
Identifiers
Symbol	ATP-synt_ab_N
Pfam	PF02874
InterPro	IPR004100
PROSITE	PDOC00137
SCOP2	1bmf / SCOPe / SUPFAM
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1fx0 B:23-95 1kmh B:23-95 1nvz A:6-73 1sky E:6-80 1e1r D:63-129 1bmf D:63-129 1nbm D:63-129 1cow F:63-129 1h8e E:63-129 1efr E:63-129 1h8h F:63-129 1w0k D:63-129 1e1q E:63-129 1w0j E:63-129 1e79 E:63-129 1e16 A:4-70 1e1i A:4-70 1v0i A:26-91 2bn9 A:21-92

Last updated August 19, 2021

ATP synthase alpha/beta chain, C terminal domain

Identifiers

Symbol

ATP-synt_ab_C

Pfam

PF00306

InterPro

IPR000793

SCOP2

1bmf / SCOPe / SUPFAM

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1e79 B:427-531 1w0j B:427-531 1h8e A:427-531 1h8h A:427-531 1efr A:427-531 1bmf B:427-531 1e1q B:427-531 1cow A:427-531 1e1r B:427-531 1w0k B:427-531 1nbm C:427-531 1sky B:376-480 1kmh A:377-495 1fx0 A:377-495 1e16 A:361-454 1e1i A:361-454 1nvz A:362-466

The alpha and beta (or A and B) subunits are found in the F1, V1, and A1 complexes of F-, V- and A-ATPases, respectively, as well as flagellar (T3SS) ATPase and the termination factor Rho. The subunits make up a ring that contains the ATP-hydrolyzing (or producing) catalytic core. The F-ATPases (or F1Fo ATPases), V-ATPases (or V1Vo ATPases) and A-ATPases (or A1Ao ATPases) are composed of two linked complexes: the F1, V1 or A1 complex containsthat synthesizes/hydrolyses ATP, and the Fo, Vo or Ao complex that forms the membrane-spanning pore. The F-, V- and A-ATPases all contain rotary motors, one that drives proton translocation across the membrane and one that drives ATP synthesis/hydrolysis.^[1]^[2]

ATPases (or ATP synthases) are membrane-bound enzyme complexes/ion transporters that combine ATP synthesis and/or hydrolysis with the transport of protons across a membrane. ATPases can harness the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. Some ATPases work in reverse, using the energy from the hydrolysis of ATP to create a proton gradient.

There are different types of ATPases, which can differ in function (ATP synthesis and/or hydrolysis), structure (F-, V- and A-ATPases contain rotary motors) and in the type of ions they transport.^[3]^[4] The types with this domain include:

F-ATPases (F1Fo ATPases) are found in mitochondria, chloroplasts and bacterial plasma membranes are the prime producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).
V-ATPases (V1Vo ATPases) are primarily found in eukaryotic vacuoles, catalysing ATP hydrolysis to transport solutes and lower pH in organelles.
A-ATPases (A1Ao ATPases) are found in Archaea and function like F-ATPases.
T3SS / flagellum ATPases, which are homologous to both parts of the A/F/V rotary ATPases: strongly in the "1" part, and weakly in the "O" part.^[5]
Ring-shaped DNA helicases like the Rho factor, where the ring is homologus to the α/β subunits.^[6]

In F-ATPases, there are three copies each of the alpha and beta subunits that form the catalytic core of the F1 complex, while the remaining F1 subunits (gamma, delta, epsilon) form part of the stalks. There is a substrate-binding site on each of the alpha and beta subunits, those on the beta subunits being catalytic, while those on the alpha subunits are regulatory. The alpha and beta subunits form a cylinder that is attached to the central stalk. The alpha/beta subunits undergo a sequence of conformational changes leading to the formation of ATP from ADP, which are induced by the rotation of the gamma subunit, itself is driven by the movement of protons through the Fo complex C subunit.^[7]

In V- and A-ATPases, the alpha/A and beta/B subunits of the V1 or A1 complex are homologous to the alpha and beta subunits in the F1 complex of F-ATPases, except that the alpha subunit is catalytic and the beta subunit is regulatory.

The alpha/A and beta/B subunits can each be divided into three regions, or domains, centred on the ATP-binding pocket, and based on structure and function. The central domain contains the nucleotide-binding residues that make direct contact with the ADP/ATP molecule.^[8]

Human proteins containing this domain

ATP5A1; ATP5B; ATP6V1A; ATP6V1B1; ATP6V1B2;

Related Research Articles

ATPases (EC 3.6.1.3, adenylpyrophosphatase, ATP monophosphatase, triphosphatase, SV40 T-antigen, adenosine 5'-triphosphatase, ATP hydrolase, complex V (mitochondrial electron transport), (Ca²⁺ + Mg²⁺)-ATPase, HCO₃⁻-ATPase, adenosine triphosphatase) are a class of enzymes that catalyze the decomposition of ATP into ADP and a free phosphate ion or the inverse reaction. This dephosphorylation reaction releases energy, which the enzyme (in most cases) harnesses to drive other chemical reactions that would not otherwise occur. This process is widely used in all known forms of life.

ATP synthase is a protein that catalyzes the formation of the energy storage molecule adenosine triphosphate (ATP) using adenosine diphosphate (ADP) and inorganic phosphate (P_i). It is classified under ligases as it changes ADP by the formation of P-O bond (phosphodiester bond). The overall reaction catalyzed by ATP synthase is:

F-ATPase, also known as F-Type ATPase, is an ATPase/synthase found in bacterial plasma membranes, in mitochondrial inner membranes, and in chloroplast thylakoid membranes. It uses a proton gradient to drive ATP synthesis by allowing the passive flux of protons across the membrane down their electrochemical gradient and using the energy released by the transport reaction to release newly formed ATP from the active site of F-ATPase. Together with V-ATPases and A-ATPases, F-ATPases belong to superfamily of related rotary ATPases.

V-ATPase Family of transport protein complexes

Vacuolar-type ATPase (V-ATPase) is a highly conserved evolutionarily ancient enzyme with remarkably diverse functions in eukaryotic organisms. V-ATPases acidify a wide array of intracellular organelles and pump protons across the plasma membranes of numerous cell types. V-ATPases couple the energy of ATP hydrolysis to proton transport across intracellular and plasma membranes of eukaryotic cells. It is generally seen as the polar opposite of ATP synthase because ATP synthase is a proton channel that uses the energy from a proton gradient to produce ATP. V-ATPase however, is a proton pump that uses the energy from ATP hydrolysis to produce a proton gradient.

MT-ATP8 is a mitochondrial gene with the full name 'mitochondrially encoded ATP synthase membrane subunit 8' that encodes a subunit of mitochondrial ATP synthase, ATP synthase F_o subunit 8. This subunit belongs to the F_o complex of the large, transmembrane F-type ATP synthase. This enzyme, which is also known as complex V, is responsible for the final step of oxidative phosphorylation in the electron transport chain. Specifically, one segment of ATP synthase allows positively charged ions, called protons, to flow across a specialized membrane inside mitochondria. Another segment of the enzyme uses the energy created by this proton flow to convert a molecule called adenosine diphosphate (ADP) to ATP. Subunit 8 differs in sequence between Metazoa, plants and Fungi.

ATPase, subunit C of Fo/Vo complex is the main transmembrane subunit of V-type, A-type and F-type ATP synthases. Subunit C was found in the Fo or Vo complex of F- and V-ATPases, respectively. The subunits form an oligomeric c ring that make up the Fo/Vo/Ao rotor, where the actual number of subunits vary greatly among specific enzymes.

ATP synthase F1 subunit alpha, mitochondrial is an enzyme that in humans is encoded by the ATP5F1A gene.

ATP synthase-coupling factor 6, mitochondrial is an enzyme subunit that in humans is encoded by the ATP5PF gene.

The ATP5MF gene encodes the ATP synthase subunit f, mitochondrial enzyme in humans.

ATP synthase delta subunit is a subunit of bacterial and chloroplast F-ATPase/synthase. It is known as OSCP in mitochondrial ATPase.

ATP synthase subunit g, mitochondrial is an enzyme that in humans is encoded by the ATP5MG gene.

Gamma subunit of ATP synthase F1 complex forms the central shaft that connects the Fo rotary motor to the F1 catalytic core. F-ATP synthases are composed of two linked complexes: the F1 ATPase complex is the catalytic core and is composed of 5 subunits, while the Fo ATPase complex is the membrane-embedded proton channel that is composed of at least 3 subunits (A-C), nine in mitochondria.

The human ATP5F1C gene encodes the gamma subunit of an enzyme called mitochondrial ATP synthase.

ATP synthase subunit b, mitochondrial is an enzyme that in humans is encoded by the ATP5PB gene.

ATP synthase subunit s, mitochondrial is an enzyme that in humans is encoded by the ATP5S gene.

ATP synthase subunit e, mitochondrial is an enzyme that in humans is encoded by the ATP5ME gene.

The human gene ATP5PD encodes subunit d of the peripheral stalk part of the enzyme mitochondrial ATP synthase.

ATP synthase subunit delta, mitochondrial, also known as ATP synthase F1 subunit delta or F-ATPase delta subunit is an enzyme that in humans is encoded by the ATP5F1D gene. This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation.

ATP synthase F1 subunit epsilon, mitochondrial is an enzyme that in humans is encoded by the ATP5F1E gene. The protein encoded by ATP5F1E is a subunit of ATP synthase, also known as Complex V. Variations of this gene have been associated with mitochondrial complex V deficiency, nuclear 3 (MC5DN3) and Papillary Thyroid Cancer.

In the field of enzymology, a proton ATPase is an enzyme that catalyzes the following chemical reaction:

References

↑ Itoh H, Yoshida M, Yasuda R, Noji H, Kinosita K (2001). "Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase". Nature. 410 (6831): 898–904. Bibcode:2001Natur.410..898Y. doi:10.1038/35073513. PMID 11309608. S2CID 3274681.
↑ Wilkens S, Zheng Y, Zhang Z (2005). "A structural model of the vacuolar ATPase from transmission electron microscopy". Micron. 36 (2): 109–126. doi:10.1016/j.micron.2004.10.002. PMID 15629643.
↑ Muller V, Cross RL (2004). "The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio". FEBS Lett. 576 (1): 1–4. doi: 10.1016/j.febslet.2004.08.065 . PMID 15473999. S2CID 25800744.
↑ Zhang X, Niwa H, Rappas M (2004). "Mechanisms of ATPases--a multi-disciplinary approach". Curr Protein Pept Sci. 5 (2): 89–105. doi:10.2174/1389203043486874. PMID 15078220.
↑ Imada, Katsumi; Minamino, Tohru; Uchida, Yumiko; Kinoshita, Miki; Namba, Keiichi (29 March 2016). "Insight into the flagella type III export revealed by the complex structure of the type III ATPase and its regulator". Proceedings of the National Academy of Sciences. 113 (13): 3633–3638. doi: 10.1073/pnas.1524025113 . PMC 4822572 . PMID 26984495.
↑ Skordalakes, Emmanuel; Berger, James M (July 2003). "Structure of the Rho Transcription Terminator". Cell. 114 (1): 135–146. doi: 10.1016/S0092-8674(03)00512-9 . PMID 12859904. S2CID 5765103.
↑ Amzel LM, Bianchet MA, Leyva JA (2003). "Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review)". Mol. Membr. Biol. 20 (1): 27–33. doi:10.1080/0968768031000066532. PMID 12745923. S2CID 218895820.
↑ Chandler D, Wang H, Antes I, Oster G (2003). "The unbinding of ATP from F1-ATPase". Biophys. J. 85 (2): 695–706. Bibcode:2003BpJ....85..695A. doi:10.1016/S0006-3495(03)74513-5. PMC 1303195 . PMID 12885621.

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[PUB00009752-1] Itoh H, Yoshida M, Yasuda R, Noji H, Kinosita K (2001). "Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase". Nature. 410 (6831): 898–904. Bibcode:2001Natur.410..898Y. doi:10.1038/35073513. PMID 11309608. S2CID 3274681.

[PUB00020609-2] Wilkens S, Zheng Y, Zhang Z (2005). "A structural model of the vacuolar ATPase from transmission electron microscopy". Micron. 36 (2): 109–126. doi:10.1016/j.micron.2004.10.002. PMID 15629643.

[PUB00020603-3] Muller V, Cross RL (2004). "The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio". FEBS Lett. 576 (1): 1–4. doi: 10.1016/j.febslet.2004.08.065 . PMID 15473999. S2CID 25800744.

[PUB00020604-4] Zhang X, Niwa H, Rappas M (2004). "Mechanisms of ATPases--a multi-disciplinary approach". Curr Protein Pept Sci. 5 (2): 89–105. doi:10.2174/1389203043486874. PMID 15078220.

[5] Imada, Katsumi; Minamino, Tohru; Uchida, Yumiko; Kinoshita, Miki; Namba, Keiichi (29 March 2016). "Insight into the flagella type III export revealed by the complex structure of the type III ATPase and its regulator". Proceedings of the National Academy of Sciences. 113 (13): 3633–3638. doi: 10.1073/pnas.1524025113 . PMC 4822572 . PMID 26984495.

[6] Skordalakes, Emmanuel; Berger, James M (July 2003). "Structure of the Rho Transcription Terminator". Cell. 114 (1): 135–146. doi: 10.1016/S0092-8674(03)00512-9 . PMID 12859904. S2CID 5765103.

[PUB00020611-7] Amzel LM, Bianchet MA, Leyva JA (2003). "Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review)". Mol. Membr. Biol. 20 (1): 27–33. doi:10.1080/0968768031000066532. PMID 12745923. S2CID 218895820.

[PUB00020612-8] Chandler D, Wang H, Antes I, Oster G (2003). "The unbinding of ATP from F1-ATPase". Biophys. J. 85 (2): 695–706. Bibcode:2003BpJ....85..695A. doi:10.1016/S0006-3495(03)74513-5. PMC 1303195 . PMID 12885621.

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