Skip to main content
. Author manuscript; available in PMC: 2020 Jan 12.
Published in final edited form as: Science. 2019 Jul 11;365(6449):185–189. doi: 10.1126/science.aaw6718

Fig. 2. Coevolution in known protein complexes.

Fig. 2.

The extent of coevolution is higher in complexes with fewer subunits (A) and varies with the function of the complexes (B). (C to E) Obligate and transient interactions revealed by coevolution provide insights into function. Bars connecting coevolving residues are in green if an experimental structure containing the interface has been determined and in red if not. Black arrows indicate inferred movements of proteins. (C) LPS transporter consisting of periplasmic LPS-binding protein LptA (orange), LptE (yellow), and outer-membrane β-barrel LptD (light blue). (D) Acetyl-CoA carboxylase complex consisting of biotin carboxylase (AccC, yellow), biotin carboxyl carrier (AccB, pink), and carboxyltransferase subunits (AccA and AccD, light blue and orange). (E) Self-inhibitory mechanism of DNA polymerase V (umuD2C). The magenta β-strand in umuD (yellow, top) is cleaved upon activation by RecA. The remaining umuD’ dimerizes (bottom) and causes the green β strand blocking the active site (black spheres below the magenta strand) in umuC (light blue) to move away and release inhibition of polymerase activity.