Solution structure of the epsilon subunit chimera combining the N-terminal beta-sandwich domain from T. Elongatus bp-1 f1 and the C-terminal alpha-helical domain from spinach chloroplast F1
ATPE_THEVB Produces ATP from ADP in the presence of a proton gradient across the membrane.[1] The complex from the organism is particularly stable to disruption and remains functional after 6 hours at 55 degrees Celsius.[2]ATPE_SPIOL Produces ATP from ADP in the presence of a proton gradient across the membrane.[HAMAP-Rule:MF_00530]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
↑Suhai T, Dencher NA, Poetsch A, Seelert H. Remarkable stability of the proton translocating F1FO-ATP synthase from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1. Biochim Biophys Acta. 2008 Apr;1778(4):1131-40. Epub 2007 Dec 31. PMID:18206981 doi:https://dx.doi.org/S0005-2736(07)00467-1
↑Suhai T, Dencher NA, Poetsch A, Seelert H. Remarkable stability of the proton translocating F1FO-ATP synthase from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1. Biochim Biophys Acta. 2008 Apr;1778(4):1131-40. Epub 2007 Dec 31. PMID:18206981 doi:https://dx.doi.org/S0005-2736(07)00467-1