The transmembrane helices of the L, M, and N subunits of Complex I from E. coli can be assigned on the basis of conservation and hydrophobic moment analysis

An assignment of the transmembrane helices of subunits L, M, and N of the Escherichia coli Complex I has been made from the helices as determined in a recent crystal structure [Efromov et al., Nature (2010) 465, 441–446]. The amino acid sequences of the three subunits were evaluated for hydrophobicity, and hydrophobic moments, to identify the helices that are likely to be in contact with membrane lipids. Using 29 closely related species, a similar analysis of average conservation, and conservation moments was performed. In each subunit, transmembrane helices 9 and 12 are predicted to form the discontinuous helices, which are likely to play a key role in function.

► Transmembrane helices of L, M, and N subunits of Complex I were assigned.
► Sequence conservation and hydrophobicity were considered in the assignments.
► Hydrophobic moment analysis identified the discontinuous transmembrane helices.
► Previously analyzed mutations were placed into the model.