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]
- ^ 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. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1220925.
- ^ a b "Entrez Gene: ATP5E ATP synthase, H+ transporting, mitochondrial F1 complex, epsilon subunit". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=514.
- ^ 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.
- Viñas O, Powell SJ, Runswick MJ, et al. (1990). "The epsilon-subunit of ATP synthase from bovine heart mitochondria. Complementary DNA sequence, expression in bovine tissues and evidence of homologous sequences in man and rat.". Biochem. J. 265 (2): 321–6. PMC 1136890. PMID 2137333. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1136890.
- Elston T, Wang H, Oster G (1998). "Energy transduction in ATP synthase.". Nature 391 (6666): 510–3. DOI:10.1038/35185. PMID 9461222.
- Wang H, Oster G (1998). "Energy transduction in the F1 motor of ATP synthase.". Nature 396 (6708): 279–82. DOI:10.1038/24409. PMID 9834036.
- Hu RM, Han ZG, Song HD, et al. (2000). "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning.". Proc. Natl. Acad. Sci. U.S.A. 97 (17): 9543–8. DOI:10.1073/pnas.160270997. PMC 16901. PMID 10931946. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=16901.
- Gross C, Kussmann S, Hehr A, et al. (2001). "Epsilon subunit gene of F(1)F(0)-ATP synthase (ATP5E) on human chromosome 20q13.2→q13.3 localizes between D20S171 and GNAS1.". Cytogenet. Cell Genet. 91 (1-4): 105–6. DOI:10.1159/000056828. PMID 11173840.
- Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865–71. DOI:10.1038/414865a. PMID 11780052.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. DOI:10.1073/pnas.242603899. PMC 139241. PMID 12477932. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Cross RL (2004). "Molecular motors: turning the ATP motor.". Nature 427 (6973): 407–8. DOI:10.1038/427407b. PMID 14749816.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. DOI:10.1101/gr.2596504. PMC 528928. PMID 15489334. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
PDB gallery
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1e79: BOVINE F1-ATPASE INHIBITED BY DCCD (DICYCLOHEXYLCARBODIIMIDE)
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1h8e: (ADP.ALF4)2(ADP.SO4) BOVINE F1-ATPASE (ALL THREE CATALYTIC SITES OCCUPIED)
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2ck3: AZIDE INHIBITED BOVINE F1-ATPASE
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2jdi: GROUND STATE STRUCTURE OF F1-ATPASE FROM BOVINE HEART MITOCHONDRIA (BOVINE F1-ATPASE CRYSTALLISED IN THE ABSENCE OF AZIDE)
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This article incorporates text from the public domain Pfam and InterPro IPR006721