Fig. 8: Sequence and structural comparison of Pcc2 and Gon7/C14 proteins.

A Structural comparison of PaPcc1-PaPcc2 and human LAGE3-C14 heterodimers. Superimposition of the crystallographic PaPcc1-PaPcc2 structures (in blue and orange, respectively) on LAGE3-C14 (in light blue and grey, respectively). The left part is a top view showing the continuous 5-strand and 6-strand β antiparallel sheets stabilising the two interfaces in LAGE3-C14 and PaPcc1-PaPcc2 complexes. The right part is a side view showing the α helices that also contribute to the building of the interfaces. B Multiple sequence alignment of Pcc1, Pcc2, C14 and Gon7 proteins from representative metazoan (H. sapiens, M. musculus), fungal (S. cerevisiae, C. glabrata) and archaeal (P. abyssi, P. furiosus) species. Red star denotes the N⁷², S/T⁷³ and D/E⁷², D/E⁷³ motifs characteristic for Pcc1 and Pcc2 paralogs, respectively. Secondary structure distribution of Pcc1 from Pyrococcus furiosus (3ENC) and of Pcc2 from Pyrococcus abyssi (7A66) are shown above and below the alignment, respectively. The residues are colored according to their physico-chemical properties. The positions with global similarity score higher that the threshold value of 0.7 are framed in blue. Multiple alignment with an extended set of representative sequences is shown in Supplementary Fig. 9.