4emm

Crystal structure of Staphylococcus aureus ClpP in compact conformationCrystal structure of Staphylococcus aureus ClpP in compact conformation

FunctionFunction

[CLPP_STAAW] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity).

About this StructureAbout this Structure

4emm is a 14 chain structure with sequence from Staaw. Full crystallographic information is available from OCA.

ReferenceReference

^{[xtra 1]}

↑ Ye F, Zhang J, Liu H, Hilgenfeld R, Zhang R, Kong X, Li L, Lu J, Zhang X, Li D, Jiang H, Yang CG, Luo C. Helix unfolding/refolding characterizes the functional dynamics of Staphylococcus aureus Clp protease. J Biol Chem. 2013 Jun 14;288(24):17643-53. doi: 10.1074/jbc.M113.452714. Epub, 2013 Apr 26. PMID:23625918 doi:http://dx.doi.org/10.1074/jbc.M113.452714

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Ye F, Zhang J, Liu H, Hilgenfeld R, Zhang R, Kong X, Li L, Lu J, Zhang X, Li D, Jiang H, Yang CG, Luo C. Helix unfolding/refolding characterizes the functional dynamics of Staphylococcus aureus Clp protease. J Biol Chem. 2013 Jun 14;288(24):17643-53. doi: 10.1074/jbc.M113.452714. Epub, 2013 Apr 26. PMID:23625918 doi:http://dx.doi.org/10.1074/jbc.M113.452714

[xtra 1]