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30  structures 257  species 3  interactions 309  sequences 6  architectures

Family: ATP-synt_Eps (PF04627)

Summary: Mitochondrial ATP synthase epsilon chain

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This is the Wikipedia entry entitled "ATP5E". More...

ATP5E Edit Wikipedia article

ATP synthase, H+ transporting, mitochondrial F1 complex, epsilon subunit

PDB rendering based on 1e79.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols ATP5E; ATPE; MC5DN3
External IDs OMIM606153 HomoloGene128187 GeneCards: ATP5E Gene
EC number 3.6.3.14
RNA expression pattern
PBB GE ATP5E 217801 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 514 n/a
Ensembl ENSG00000124172 n/a
UniProt P56381 n/a
RefSeq (mRNA) NM_006886 n/a
RefSeq (protein) NP_008817 n/a
Location (UCSC) Chr 20:
57.6 – 57.61 Mb
n/a
PubMed search [1] n/a
Mitochondrial ATP synthase epsilon chain
PDB 2jdi EBI.jpg
ground state structure of f1-atpase from bovine heart mitochondria (bovine f1-atpase crystallised in the absence of azide)
Identifiers
Symbol ATP-synt_Eps
Pfam PF04627
InterPro IPR006721
SCOP 1e79
SUPERFAMILY 1e79

ATP synthase subunit epsilon, mitochondrial is an enzyme that in humans is encoded by the ATP5E gene.[1][2]

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 is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3. The proton channel consists of three main subunits (a, b, c). This gene encodes the epsilon subunit of the catalytic core. Two pseudogenes of this gene are located on chromosomes 4 and 13.[2]

The epsilon subunit is located in the stalk region of the F1 complex, and acts as an inhibitor of the ATPase catalytic core. The epsilon subunit can assume two conformations, contracted and extended, where the latter inhibits ATP hydrolysis. The conformation of the epsilon subunit is determined by the direction of rotation of the gamma subunit, and possibly by the presence of ADP. The extended epsilon subunit is thought to become extended in the presence of ADP, thereby acting as a safety lock to prevent wasteful ATP hydrolysis.[3]

References[edit]

  1. ^ Tu Q, Yu L, Zhang P, Zhang M, Zhang H, Jiang J, Chen C, Zhao S (Jun 2000). "Cloning, characterization and mapping of the human ATP5E gene, identification of pseudogene ATP5EP1, and definition of the ATP5E motif". Biochem J. 347 Pt 1: 17–21. PMC 1220925. PMID 10727396. 
  2. ^ a b "Entrez Gene: ATP5E ATP synthase, H+ transporting, mitochondrial F1 complex, epsilon subunit". 
  3. ^ Feniouk BA, Junge W (September 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): 5114–8. doi:10.1016/j.febslet.2005.08.030. PMID 16154570. 

Further reading[edit]


This article incorporates text from the public domain Pfam and InterPro IPR006721

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

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Mitochondrial ATP synthase epsilon chain Provide feedback

This family constitutes the mitochondrial ATP synthase epsilon subunit. This is not to be confused with the bacterial epsilon subunit, which is homologous to the mitochondrial delta subunit (PF00401 and PF02823) The epsilon subunit is located in the extrinsic membrane section F1, which is the catalytic site of ATP synthesis. The epsilon subunit was not well ordered in the crystal structure of bovine F1 [1] but it is known to be located in the stalk region of F1 [2]. E subunit is thought to be involved in the regulation of ATP synthase, since a null mutation increased oligomycin sensitivity and decreased inhibition by inhibitor protein IF1 [2].

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

  2. Tu Q, Yu L, Zhang P, Zhang M, Zhang H, Jiang J, Chen C, Zhao S; , Biochem J 2000;347:17-21.: Cloning, characterization and mapping of the human ATP5E gene, identification of pseudogene ATP5EP1, and definition of the ATP5E motif. PUBMED:10727396 EPMC:10727396


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR006721

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.

This family constitutes the mitochondrial ATP synthase epsilon subunit, which is distinct from the bacterial epsilon subunit (the latter being homologous to the mitochondrial delta subunit, INTERPRO). The mitochondrial epsilon subunit is located in the stalk region of the F1 complex, and acts as an inhibitor of the ATPase catalytic core. The epsilon subunit can assume two conformations, contracted and extended, where the latter inhibits ATP hydrolysis. The conformation of the epsilon subunit is determined by the direction of rotation of the gamma subunit, and possibly by the presence of ADP. The extended epsilon subunit is thought to become extended in the presence of ADP, thereby acting as a safety lock to prevent wasteful ATP hydrolysis [PUBMED:16154570].

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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Representative proteomes NCBI
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Meta
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(63)
RP35
(113)
RP55
(163)
RP75
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  Seed
(30)
Full
(309)
Representative proteomes NCBI
(292)
Meta
(1)
RP15
(63)
RP35
(113)
RP55
(163)
RP75
(199)
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Seed source: DOMO:DM04624;
Previous IDs: ATP-synt_E;
Type: Family
Author: Kerrison ND
Number in seed: 30
Number in full: 309
Average length of the domain: 49.00 aa
Average identity of full alignment: 38 %
Average coverage of the sequence by the domain: 53.74 %

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 20.5 20.5
Trusted cut-off 21.8 20.9
Noise cut-off 18.4 18.4
Model length: 50
Family (HMM) version: 8
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Interactions

There are 3 interactions for this family. More...

ATP-synt_DE ATP-synt_DE_N 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_Eps domain has been found. There are 30 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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