Figure 2 | Scientific Reports

Figure 2

From: Molecular insights into the dynamic modulation of bacterial ClpP function and oligomerization by peptidomimetic boronate compounds

Figure 2

(a) ClustalW sequence alignment with SeClpP and S. aureus ClpP (SaClpP) amino acid sequences in FASTA format; (b) catalytic site of a monomer from the SeClpP-ixazomib complex and interactions between ixazomib and residues in the catalytic cleft. The amino acids that form hydrogen bonds with the ligand are labeled and colored in orange. Ixazomib is shown with the 2Fo-Fc electron density at 1.5σ. All the ClpP monomers bound to the ligand are shown in Supplementary Fig. S1. Comparison between the Gly-rich regions of different crystal structures of ClpP: (c) apo SeClpP with its partially disordered Gly-rich region; (d) SeClpP-ixazomib complex with its ordered Gly-rich region (two antiparallel beta-strands); (e) SaClpP-AV145 complex with its disordered, or unstructured, Gly-rich region.

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