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Figure 1
Site-directed mutagenesis disrupts crystal packing involving active-site surface loops. (a) Sequence alignment of P. aeruginosa DsbA1 with homologues from E. coli, K. pneumoniae and V. cholerae to identify a suitable nonpolar amino-acid substitution for Glu82 in P. aeruginosa (marked with an asterisk). The figure was generated using ESPript3 (Robert & Gouet, 2014BB24). Comparison of symmetry-related molecule packing in crystals of WT PaDsbA1 (b) (blue) and E82I PaDsbA1 (c) (orange) indicates reduced involvement of the active-site surface loops (shown in red for each protein) in packing interactions in E82I PaDsbA1 relative to WT PaDsbA1.

Journal logoBIOLOGICAL
ISSN: 1399-0047
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