We have determined all known atomic structures of complex I, starting from the hydrophilic domain of Thermus thermophilus enzyme (eight subunits, nine Fe — S clusters), followed by the membrane domains of the Escherichia coli (six subunits, 55
transmembrane helices) and T. thermophilus (seven subunits, 64
transmembrane helices) enzymes, and finally culminating in a recent crystal structure of the entire intact complex I from T. thermophilus (536 kDa, 16 subunits, nine Fe — S clusters, 64
transmembrane helices).
This structure could represent a stretch activated state of TREK - 2, where mechanical force applied to the lipid membrane leads to an upward movement in
transmembrane helices M2 - M4 into this up conformation.
This process has been exploited to assess the energetics of
transmembrane -
helices, as described in two recent studies by the von Heijne and White groups (published here and elsewhere).