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. 2021 Apr 29;11:673122. doi: 10.3389/fcimb.2021.673122

Figure 1.

Figure 1

IpgC/IpaB available structural information. (A) A schematic representation of the IpaB full-length protein and the available structural information. The long coiled-coil domain of IpaB (green rectangle, residues 74 - 239) is the only known domain in atomic resolution along with the Chaperone Binding Domain (CBD, magenta rectangle, residues 60-72). The CBD domain was found in extended conformation interacting with the major groove of one IpgC molecule (cartoon representation, blue monomer). See text for details. Other segments of IpaB were proposed as being implicated in the interaction with IpgC: a second CBD (red rectangle) at the N-terminal of IpaB; and an extension of the first CBD (pink rectangle). Grey rectangles on bottom of IpaB sequence represent predicted α-helices. (B) Constraint-based Multiple Alignment, COBALT (Papadopoulos and Agarwala, 2007). Part of the alignment, focusing on the C-terminal part of major translocators from T3S systems of different origin, is presented. Multiple sequence alignment columns with no gaps are colored. Higher conserved columns in red, less conserved ones in blue and non-conserved in grey. Accession numbers for the protein sequences used are provided in Materials and Methods section Modeling of the IpgC/IpaB Complex.