Homology modeling suggests that a selected mutation in an ABC transporter transmembrane domain (Cphy 2465) in cellulose-adapted populations occurs at a protein-protein interface.

<p>The maltose transporter (3pv0) is shown because its transmembrane domains MalF (green) and MalG (magenta) are the best templates of known structure for Cphy 2465 and Cphy 2464, respectively. A homology model of Cphy 2465 based on MalF places the selected A207V mutation (red) in the coupling helix (arrow and table) that is important in transmitting changes between the transmembrane domains (green and magenta) and the ATPase domains (blue and gold). The mutation occurs in the consensus sequence originally identified in several transporters <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0086731#pone.0086731-Dassa1" target="_blank">[45]</a>.