ATP:ADP antiporter family
The ATP:ADP Antiporter (AAA) Family (TC# 2.A.12) is a member of the major facilitator superfamily. Members of the AAA family have been sequenced from bacteria and plants.[1]
Structure and function
[edit]One protein from the obligate intracellular bacterial parasite, Rickettsia prowazekii, is of 498 amino acyl residues, and is believed to span the membrane 12 times.[2] The transporter is an obligate exchange translocase specific for ATP and ADP. It functions to take up ATP from the eukaryotic cell cytoplasm into the bacterium in exchange for ADP. The ATP/ADP uniporters can also transport inorganic phosphate, but not ribonucleoside and monophosphates, as well as deoxyribonucleotides.[3][4]
Transport reaction
[edit]The transport reaction catalyzed by the antiporters is:
ATP (out) + ADP (in) ⇌ ATP (in) + ADP (out)
Homology
[edit]The AAA family proteins are distantly related to members of the major facilitator superfamily, and are not related to the mitochondrial ATP/ADP exchangers of the mitochondrial carrier family which pump ATP out of mitochondria in accordance with the polarity of the mitochondrial membrane potential.
References
[edit]- ^ Winkler, H. H.; Neuhaus, H. E. (1999-02-01). "Non-mitochondrial ATP transport". Trends in Biochemical Sciences. 24 (2): 64–68. doi:10.1016/s0968-0004(98)01334-6. ISSN 0968-0004. PMID 10098400.
- ^ Alexeyev, Mikhail (29 Jan 1999). "Membrane topology of the Rickettsia prowazekii ATP/ADP translocase revealed by novel dual pho-lac reporters". Journal of Molecular Biology. 285 (4): 1503–13. doi:10.1006/jmbi.1998.2412. PMID 9917392.
- ^ Trentmann, Oliver; Jung, Benjamin; Neuhaus, Horst Ekkehard; Haferkamp, Ilka (2008-12-26). "Nonmitochondrial ATP/ADP transporters accept phosphate as third substrate". The Journal of Biological Chemistry. 283 (52): 36486–36493. doi:10.1074/jbc.M806903200. ISSN 0021-9258. PMC 2606016. PMID 19001371.
- ^ Tjaden, Joachim (Feb 1999). "wo nucleotide transport proteins in Chlamydia trachomatis, one for net nucleoside triphosphate uptake and the other for transport of energy". Journal of Bacteriology. 181 (4): 1196–202. doi:10.1128/JB.181.4.1196-1202.1999. PMC 93497. PMID 9973346.
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