Extended Data Fig. 2: Sequence alignment of representative AvrE-family effectors.
From: Bacterial pathogens deliver water- and solute-permeable channels to plant cells
Sequences of E. amylovora DspE, P. carotovorum DspE, Pst DC3000 AvrE, and P. stewartii WtsE are aligned using Clustal Omega44. Domain regions are indicated above the aligned sequences. Sequence identities between different protein pairs are labeled. The β-barrel is formed with multiple helices and long loops inserted within the primary sequence of the β-barrel. In E. amylovora DspE, the β-barrel starts from a small β-hairpin from K932-E956, which is followed by a large insertion of multiple helices (including a vertical helix bundle) from E957-D1276. The main β-barrel follows from S1277-G1813, though it is disrupted by several insertion loops and helices, including T1403-E1430 (a helix-turn-helix motif), A1567-H1647 (a horizontal helix bundle), N1662-P1712 (an insertion loop followed by a helix-turn-helix motif), and K1723-N1753 (two antiparallel helices). The β-barrel is further appended with a C-terminal helix and an extended loop (G1814-S1838). Mutated outward-facing residues (L1776, L1777, and L1778) and inward-facing residues (K1399 and K1401) of the β-barrel are labeled in pink and blue, respectively.
