7KLD

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

7KLD の概要

• エントリーDOI: 10.2210/pdb7kld/pdb
• 関連するBIRD辞書のPRD_ID: PRD_002454
• 分子名称: Phage-related ribosomal protease, LYS-LEU-ASN-LEU-GLN-PHE-PCS, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: cysteine protease ribosomal protein l27, hydrolase, product complex
• 由来する生物種: Staphylococcus aureus; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 38253.80

構造登録者

Wright, H.T.,Peterson, D. (登録日: 2020-10-29, 公開日: 2021-09-01, 最終更新日: 2023-10-25)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.25 Å)