4RR0

re-refined 1vcw, CRYSTAL STRUCTURE OF DEGS AFTER BACKSOAKING THE ACTIVATING PEPTIDE

4RR0 の概要

• エントリーDOI: 10.2210/pdb4rr0/pdb
• 分子名称: Protease degS (2 entities in total)
• 機能のキーワード: stress response, protein quality control, pdz, upr, htra, hydrolase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 99730.99

構造登録者

Sauer, R.T.,Grant, R.A. (登録日: 2014-11-05, 公開日: 2015-03-11, 最終更新日: 2024-02-28)

主引用文献

de Regt, A.K.,Kim, S.,Sohn, J.,Grant, R.A.,Baker, T.A.,Sauer, R.T.
A Conserved Activation Cluster Is Required for Allosteric Communication in HtrA-Family Proteases.
Structure, 23:517-526, 2015

PubMed Abstract: In E. coli, outer-membrane stress causes a transcriptional response through a signaling cascade initiated by DegS cleavage of a transmembrane antisigma factor. Each subunit of DegS, an HtrA-family protease, contains a protease domain and a PDZ domain. The trimeric protease domain is autoinhibited by the unliganded PDZ domains. Allosteric activation requires binding of unassembled outer-membrane proteins (OMPs) to the PDZ domains and protein substrate binding. Here, we identify a set of DegS residues that cluster together at subunit-subunit interfaces in the trimer, link the active sites and substrate binding sites, and are crucial for stabilizing the active enzyme conformation in response to OMP signaling. These residues are conserved across the HtrA-protease family, including orthologs linked to human disease, supporting a common mechanism of allosteric activation. Indeed, mutation of residues at homologous positions in the DegP quality-control protease also eliminates allosteric activation.

PubMed: 25703375
DOI: 10.1016/j.str.2015.01.012

実験手法

X-RAY DIFFRACTION (3.054 Å)