Ontology highlight
ABSTRACT:
SUBMITTER: Shen QT
PROVIDER: S-EPMC2660739 | biostudies-literature | 2009 Mar
REPOSITORIES: biostudies-literature
Shen Qing-Tao QT Bai Xiao-Chen XC Chang Lei-Fu LF Wu Yi Y Wang Hong-Wei HW Sui Sen-Fang SF
Proceedings of the National Academy of Sciences of the United States of America 20090302 12
In the periplasm of Escherichia coli, DegP (also known as HtrA), which has both chaperone-like and proteolytic activities, prevents the accumulation of toxic misfolded and unfolded polypeptides. In solution, upon binding to denatured proteins, DegP forms large cage-like structures. Here, we show that DegP forms a range of bowl-shaped structures, independent of substrate proteins, each with a 4-, 5-, or 6-fold symmetry and all with a DegP trimer as the structural unit, on lipid membranes. These m ...[more]