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59  structures 4653  species 5  interactions 5197  sequences 6  architectures

Family: ATP-synt (PF00231)

Summary: ATP synthase

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This is the Wikipedia entry entitled "ATP synthase gamma subunit". More...

ATP synthase gamma subunit Edit Wikipedia article

ATP synthase
PDB 1bmf EBI.jpg
Structure of F1-ATPase.[1]
Identifiers
Symbol ATP-synt
Pfam PF00231
InterPro IPR000131
PROSITE PDOC00138
SCOP 1bmf
SUPERFAMILY 1bmf

Gamma subunit of ATP synthase F1 complex forms the central shaft that connects the F0 rotary motor to the F1 catalytic core. F-ATP synthases (also known as F1F0-ATPase, or H(+)-transporting two-sector ATPase) (EC 3.6.3.14) are composed of two linked complexes: the F1 ATPase complex is the catalytic core and is composed of 5 subunits (alpha, beta, gamma, delta, epsilon), while the F0 ATPase complex is the membrane-embedded proton channel that is composed of at least 3 subunits (A-C), nine in mitochondria (A-G, F6, F8).

The human ATP synthase gamma subunit is encoded by the gene ATP5C1.

Molecular Interactions

Both the F1 and F0 complexes are rotary motors that are coupled back-to-back. In the F1 complex, the central gamma subunit forms the rotor inside the cylinder made of the alpha(3)beta(3) subunits, while in the F0 complex, the ring-shaped C subunits forms the rotor. The two rotors rotate in opposite directions, but the F0 rotor is usually stronger, using the force from the proton gradient to push the F1 rotor in reverse in order to drive ATP synthesis.[2] These ATPases can also work in reverse to hydrolyse ATP to create a proton gradient.

The ATPase F1 complex gamma subunit forms the central shaft that connects the F0 rotary motor to the F1 catalytic core. The gamma subunit functions as a rotary motor inside the cylinder formed by the alpha(3)beta(3) subunits in the F1 complex.[3] The best-conserved region of the gamma subunit is its C-terminus, which seems to be essential for assembly and catalysis.

References

  1. ^ Abrahams JP, Leslie AG, Lutter R, Walker JE (August 1994). "Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria". Nature 370 (6491): 621–8. doi:10.1038/370621a0. PMID 8065448. 
  2. ^ 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. doi:10.1038/35073513. PMID 11309608. 
  3. ^ Junge W, Feniouk BA (2005). "Regulation of the F0F1-ATP synthase: the conformation of subunit epsilon might be determined by directionality of subunit gamma rotation". FEBS Lett. 579 (23): 5114–5118. doi:10.1016/j.febslet.2005.08.030. PMID 16154570. 

This article incorporates text from the public domain Pfam and InterPro IPR000131

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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No Pfam abstract.

Literature references

  1. Abrahams JP, Leslie AG, Lutter R, Walker JE; , Nature 1994;370:621-628.: Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria. PUBMED:8065448 EPMC:8065448


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000131

Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing 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.

There are several different types of transmembrane ATPases, which can differ in function (ATP hydrolysis and/or synthesis), structure (e.g., F-, V- and A-ATPases, which contain rotary motors) and in the type of ions they transport [PUBMED:15473999, PUBMED:15078220]. The different types include:

  • F-ATPases (F1F0-ATPases), which are found in mitochondria, chloroplasts and bacterial plasma membranes where they are the prime producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).
  • V-ATPases (V1V0-ATPases), which are primarily found in eukaryotic vacuoles and catalyse ATP hydrolysis to transport solutes and lower pH in organelles.
  • A-ATPases (A1A0-ATPases), which are found in Archaea and function like F-ATPases (though with respect to their structure and some inhibitor responses, A-ATPases are more closely related to the V-ATPases).
  • P-ATPases (E1E2-ATPases), which are found in bacteria and in eukaryotic plasma membranes and organelles, and function to transport a variety of different ions across membranes.
  • E-ATPases, which are cell-surface enzymes that hydrolyse a range of NTPs, including extracellular ATP.

F-ATPases (also known as F1F0-ATPase, or H(+)-transporting two-sector ATPase) (EC) are composed of two linked complexes: the F1 ATPase complex is the catalytic core and is composed of 5 subunits (alpha, beta, gamma, delta, epsilon), while the F0 ATPase complex is the membrane-embedded proton channel that is composed of at least 3 subunits (A-C), nine in mitochondria (A-G, F6, F8). Both the F1 and F0 complexes are rotary motors that are coupled back-to-back. In the F1 complex, the central gamma subunit forms the rotor inside the cylinder made of the alpha(3)beta(3) subunits, while in the F0 complex, the ring-shaped C subunits forms the rotor. The two rotors rotate in opposite directions, but the F0 rotor is usually stronger, using the force from the proton gradient to push the F1 rotor in reverse in order to drive ATP synthesis [PUBMED:11309608]. These ATPases can also work in reverse to hydrolyse ATP to create a proton gradient.

The ATPase F1 complex gamma subunit forms the central shaft that connects the F0 rotary motor to the F1 catalytic core. The gamma subunit functions as a rotary motor inside the cylinder formed by the alpha(3)beta(3) subunits in the F1 complex [PUBMED:16154570]. The best-conserved region of the gamma subunit is its C terminus, which seems to be essential for assembly and catalysis.

More information about this protein can be found at Protein of the Month: ATP Synthases [PUBMED:].

Gene Ontology

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Domain organisation

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Alignments

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(161)
Full
(5197)
Representative proteomes NCBI
(3418)
Meta
(3462)
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(435)
RP35
(822)
RP55
(1071)
RP75
(1266)
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  Seed
(161)
Full
(5197)
Representative proteomes NCBI
(3418)
Meta
(3462)
RP15
(435)
RP35
(822)
RP55
(1071)
RP75
(1266)
Alignment:
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  Seed
(161)
Full
(5197)
Representative proteomes NCBI
(3418)
Meta
(3462)
RP15
(435)
RP35
(822)
RP55
(1071)
RP75
(1266)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

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Trees

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Curation and family details

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Seed source: Prosite
Previous IDs: none
Type: Domain
Author: Finn RD
Number in seed: 161
Number in full: 5197
Average length of the domain: 281.00 aa
Average identity of full alignment: 34 %
Average coverage of the sequence by the domain: 97.64 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.1 22.1
Trusted cut-off 22.4 22.4
Noise cut-off 21.7 22.0
Model length: 290
Family (HMM) version: 14
Download: download the raw HMM for this family

Species distribution

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Interactions

There are 5 interactions for this family. More...

ATP-synt_DE_N ATP-synt_ab_C ATP-synt_ab ATP-synt_Eps ATP-synt

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the ATP-synt domain has been found. There are 59 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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