Figure 1
From: Investigation of the chaperone function of the small heat shock protein — AgsA
(A) Amino-acid alignment and (B) predicted three-dimensional structure of AgsA. (A) The alignment includes the S. enterica serovar Typhimurium AgsA (GenBank: GU130588), E. coli IbpA (GenBank: BAE77607) and IbpB (GenBank: BAE77608), T. aestivum Hsp16.9 (PDB: 1GMEA), and Bos taurus α-crystallin (GenBank: NP776714). Identical and similar (L/V/I, F/Y/W/H, R/K/H, D/E, G/A, S/T) amino acid residues are shown in bold if they occur in at least 3 sequences. (B) Structure of AgsA was predicted by the Geno3 D server (PBIL, Lyon, France) using the structure of T. aestivum Hsp16.9 as a template. The α-crystallin domain (yellow), N-terminal arm (red), and C-terminal extension (blue) are distinguished by colors. The arrows indicate the position of the N- or C-terminal truncations of AgsA used in this study.