6Q12

Structure of pro-Esp mutant- S66V

6Q12 の概要

• エントリーDOI: 10.2210/pdb6q12/pdb
• 関連するPDBエントリー: 6PYM
• 分子名称: Glutamyl endopeptidase (2 entities in total)
• 機能のキーワード: serine protease, hydrolase, zymogen
• 由来する生物種: Staphylococcus epidermidis (strain ATCC 12228)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55297.02

構造登録者

Manne, K.,Narayana, S.V.L. (登録日: 2019-08-02, 公開日: 2019-08-14, 最終更新日: 2023-10-11)

主引用文献

Manne, K.,Narayana, S.V.L.
Structural insights into the role of the N-terminus in the activation and function of extracellular serine protease from Staphylococcus epidermidis.
Acta Crystallogr D Struct Biol, 76:28-40, 2020

PubMed Abstract: Extracellular serine protease (Esp) from Staphylococcus epidermidis is a glutamyl endopeptidase that inhibits the growth and formation of S. aureus biofilms. Previously, crystal structures of the matured and active Esp have been determined. Interestingly, many of the staphylococcal glutamyl endopeptidase zymogens, including V8 from Staphylococcus aureus and Esp from S. epidermidis, contain unusually long pro-peptide segments; however, their function is not known. With the aim of elucidating the function of these pro-peptide segments, crystal structures of the Esp zymogen (Pro-Esp) and its variants were determined. It was observed that the N-terminus of the Pro-Esp crystal structure is flexible and is not associated with the main body of the enzyme, unlike in the known active Esp structure. In addition, the loops that border the putative substrate-binding pocket of Pro-Esp are flexible and disordered; the structural components that are responsible for enzyme specificity and efficiency in serine proteases are disordered in Pro-Esp. However, the N-terminal locked Pro-Esp variants exhibit a rigid substrate-binding pocket similar to the active Esp structure and regain activity. These structural studies highlight the role of the N-terminus in stabilizing the structural components responsible for the activity and specificity of staphylococcal glutamyl endopeptidases.

PubMed: 31909741
DOI: 10.1107/S2059798319015055

実験手法

X-RAY DIFFRACTION (2.2 Å)