Fig. 1: Structure, conformations and domain architecture of E. coli SurA.
From: Dual client binding sites in the ATP-independent chaperone SurA
a Crystal structure of wild-type (WT) E. coli SurA (PDB: 1M5Y48) with missing residues added using MODELLER56,119. In this structure the P1 domain is bound to the core domain (named here, SurA core-P1 closed). Regions are coloured grey (N-terminal region of the core domain), green (P1), yellow (P2) and orange (C-terminal region of the core domain). This colour scheme for SurA domains is used throughout. b Model of WT SurA in which the P1 domain is extended away from the core domain (named here SurA core-P1 open). The model was built using MODELLER56,119 and the crystal structures of full-length SurA (PDB: 1M5Y48) and SurA-ΔP2 (PDB: 2PV359). c Bar chart showing the percentage of SurA homologues from the InterPro family IPRO15391 (14,422 homologues) which contain at least one PPIase domain (1+PPIase) or are core domain only (Core only) homologues. d Domain architecture of E. coli SurA-WT and the SurA domain deletion variants used in this study. The signal sequence was not present in the constructs used here, but the numbering used reflects the gene numbering and includes the signal peptide (residues 1–22) (white). Source data are provided as a Source Data file.
