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Figure 7
Bromophenoxy propanamide (1) binding requires a shift of Tyr110 to open a cryptic hydrophobic pocket. (a) Side-chain position of Tyr110 in the absence of ligand. (b) The same region in the presence of 1, showing that Tyr110 shifts up (towards helix α3), opening a binding site for 1. (c) Superposition of Tyr110 in apo and liganded conformations (fragment 1): the centre of the benzene ring of the tyrosine is displaced 2.1 Å between the two conformations. (d) Structure of the BpsDsbA–fragment 1 complex (PDB entry 7luh) showing the cryptic pocket above the catalytic active site. Fragment 1 (orange) binds in a hydrophobic pocket. All residues within 5 Å of 1 are shown as purple sticks and labelled; water molecules are shown as red spheres. The distances between different atoms or ring centromeres separated by a yellow dashed line are given in italics (in Å). The S atoms in the 43CPHC46 active site of BpsDsbA are shown as yellow sticks. α-Helices are numbered. Note that Lys108 is truncated in PDB entry 7luh as no 2mFoDFc density was visible beyond Cγ at 0.8 r.m.s.d.

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ISSN: 2059-7983
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