Figure 5 | Scientific Reports

Figure 5

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

Figure 5

Illustration of the conformation of the Asn42 sidechain in different crystal structures of ClpP: (a) SeClpP-ixazomib complex, (b) active mutant (SaClpP Y63A) (PDB ID: 5C90)29 of ClpP from Staphylococcus aureus (Sa), and (c) native SeClpP. In (a) and (b), Asn42 is in a “down” position, with open pores (active for proteolysis). In contrast, in (c), the same amino acid residue is found in the “up” position, characteristic of closed ClpP.

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