PMID:21893291
| Citation |
Bai, XC, Pan, XJ, Wang, XJ, Ye, YY, Chang, LF, Leng, D, Lei, J and Sui, SF (2011) Characterization of the structure and function of Escherichia coli DegQ as a representative of the DegQ-like proteases of bacterial HtrA family proteins. Structure 19:1328-37 |
|---|---|
| Abstract |
HtrA family proteins play a central role in protein quality control in the bacterial periplasmic space. DegQ-like proteases, a group of bacterial HtrA proteins, are characterized by a short LA loop as compared with DegP-like proteases, and are found in many bacterial species. As a representative of the DegQ-like proteases, we report that Escherichia coli DegQ exists in vivo primarily as a trimer (substrate-free) or dodecamer (substrate-containing). Biochemical analysis of DegQ dodecamers revealed that the major copurified protein substrate is OmpA. Importantly, wild-type DegQ exhibited a much lower proteolytic activity, and thus higher chaperone-like activity, than DegP. Furthermore, using cryo-electron microscopy we determined high-resolution structures of DegQ 12- and 24-mers in the presence of substrate, thus revealing the structural mechanism by which DegQ moderates its proteolytic activity. |
| Links |
PubMed Online version:10.1016/j.str.2011.06.013 |
| Keywords |
Catalytic Domain; Chromatography, Gel; Cryoelectron Microscopy; Enzyme Assays; Escherichia coli/enzymology; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/ultrastructure; Models, Molecular; Protein Binding; Protein Interaction Domains and Motifs; Protein Multimerization; Protein Structure, Quaternary; Serine Endopeptidases/chemistry; Serine Endopeptidases/ultrastructure; Surface Properties |
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