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Figure 2
Substrate recognition by PfHsp70-x SBD. (a) Electron-density (2FoFc) OMIT map of the substrate peptide bound to PfHsp70-x SBD. The map was contoured at 1σ. The protein loops L1,2 and L3,4, which define the substrate-binding groove, are indicated. The substrate peptide, which is shown as a reference but was not included in the map calculations, is represented as sticks. (b) The Ala437–Tyr462 arch forming over the substrate-binding groove is shown. The side chains of the protein residues forming this arch are denoted as spheres. (c) Surface representation of the PfHsp70-x SBD hydrophobic cavity where the peptide L5 (side chain shown as spheres) docks. The surfaces of the protein residues that are directly involved in L5 binding are coloured light blue. (d) Hydrogen bonds inferred between the substrate peptide and PfHsp70-x SBD. Protein residues participating in hydrogen bonds are shown as sticks and coloured light blue. Hydrogen bonds are shown as dashed yellow lines.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
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