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TitleCharacterization of the structure and function of Escherichia coli DegQ as a representative of the DegQ-like proteases of bacterial HtrA family proteins.
Journal, issue, pagesStructure, Vol. 19, Issue 9, Page 1328-1337, Year 2011
Publish dateSep 7, 2011
AuthorsXiao-chen Bai / Xi-jiang Pan / Xiao-jing Wang / Yun-ying Ye / Lei-fu Chang / Dong Leng / Jianlin Lei / Sen-Fang Sui /
PubMed AbstractHtrA 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 ...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.
External linksStructure / PubMed:21893291
MethodsEM (single particle)
Resolution6.5 - 8.2 Å
Structure data

EMDB-5289:
The cryo-EM map of DegQ 24-mer
Method: EM (single particle) / Resolution: 6.5 Å

EMDB-5290:
The cryo-EM map of DegQ 12-mer
Method: EM (single particle) / Resolution: 8.2 Å

Source
  • Escherichia coli (E. coli)

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