7KLD

Crystal Structure of an Essential Ribosomal Processing Protease Prp from S. aureus in complex with a covalently linked product Peptide

Summary for 7KLD

• Entry DOI: 10.2210/pdb7kld/pdb
• Related PRD ID: PRD_002454
• Descriptor: Phage-related ribosomal protease, LYS-LEU-ASN-LEU-GLN-PHE-PCS, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: cysteine protease ribosomal protein l27, hydrolase, product complex
• Biological source: Staphylococcus aureus; More
• Total number of polymer chains: 6
• Total formula weight: 38253.80

Authors

Wright, H.T.,Peterson, D. (deposition date: 2020-10-29, release date: 2021-09-01, Last modification date: 2023-10-25)

Primary citation

Hotinger, J.A.,Pendergrass, H.A.,Peterson, D.,Wright, H.T.,May, A.E.
Phage-Related Ribosomal Protease (Prp) of Staphylococcus aureus : In Vitro Michaelis-Menten Kinetics, Screening for Inhibitors, and Crystal Structure of a Covalent Inhibition Product Complex.
Biochemistry, 61:1323-1336, 2022

PubMed Abstract: Phage-related ribosomal proteases (Prps) are essential for the assembly and maturation of the ribosome in Firmicutes, including the human pathogens , , and . These bacterial proteases cleave off an N-terminal extension of a precursor of ribosomal protein L27, a processing step that is essential for the formation of functional ribosomes. This essential role of Prp in these pathogens has identified this protease as a potential antibiotic target. In this work, we determine the X-ray crystal structure of a covalent inhibition complex at 2.35 Å resolution, giving the first complete picture of the active site of a functional Prp. We also characterize the kinetic activity and screen for potential inhibitors of Prp. This work gives the most complete characterization of the structure and specificity of this novel class of proteases to date.

PubMed: 35731716
DOI: 10.1021/acs.biochem.2c00010

Experimental method

X-RAY DIFFRACTION (2.25 Å)