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. Author manuscript; available in PMC: 2012 Jun 1.
Published in final edited form as: Mol Microbiol. 2011 May 5;80(6):1530–1548. doi: 10.1111/j.1365-2958.2011.07665.x

Figure 2. The structure of E. coli SurA indicating the position of mutations introduced in this study.

Figure 2

(A) The structure of SurA was used as a guide to design mutations in PrsA2. By analogy with SurA, PrsA2 is predicted to act as a dimer with contributions from both the N and C-terminus of each monomer. PPIase domain (red), N-terminus of monomer 1 (green), N-terminus of monomer 2 (light blue), C terminus of monomer 2 (yellow and blue). Purple regions represent predicted contact regions for substrate binding in the C-terminus of monomer 2 and the N-terminus of monomer 1. (B) Amino acid sequence alignment of PrsA2 and PrsA1. Black shading indicates identical amino acids between PrsA2 and PrsA1; gray shading indicates similar amino acids; and red highlighting represents the four initial regions of the putative substrate binding cleft targeted for mutagenesis. Western blot of the nine mutants is shown (C).