Conserved domains of PilQ.
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Abstract
<p>Panel <b>A.</b> Conserved domains of MxPilQ (901 residues) and TtPilQ (757 residues) <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0070144#pone.0070144-MarchlerBauer1" target="_blank">[58]</a>. The conserved feature are drawn to scale and areindicated by shaded letters below both protein. Each has the PilQ region at their C-terminus consisting of the highly conserved Secretin domain and the region immediately N-terminal of secretin (Secretin_N). Two AMIN domains <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0070144#pone.0070144-deSouza1" target="_blank">[59]</a> are found at the N-terminus of MxPilQ but not TtPilQ. The brackets and the labels above indicate the different Y2H constructs and/or subdomains in each protein. Panel <b>B.</b> Structural alignment of the N-termini of TtPilQ and the T2SS secretin GspD from Enterotoxigenic <i>E. coli</i> (ETEC) <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0070144#pone.0070144-Kelley1" target="_blank">[50]</a>, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0070144#pone.0070144-Korotkov3" target="_blank">[55]</a>. The boundaries between N0 and N1 as well as N1 and N2 subdomains in GspD are indicated by arrows (↑). The secondary structure of GspD from crystallography and that of TtPilQ predicted from modeling are indicated below and above the aligned sequences, respectively, with β strands represented by block arrows and α helices by cylinders.</p