Structure of ClpP in complex with ADEP2 in triclinic crystal form

Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism

ATP-dependent Clp protease proteolytic subunit

Endopeptidase Clp, Caseinolytic protease, Stress protein G7

0.1M CHES, 200mM NaCl, 10% PEG 8000, pH 9.5, hanging drop, temperature 295K

CLPP in complex with ADEP2 in monoclinic crystal form

ADEP2 IS A SYNTHETIC OPTIMIZED CONGENERS OF THE NATURAL PRODUCT ADEP1

ATP-dependent Clp protease proteolytic subunit (E.C.3.4.21.92), Acyldepsipeptide 2

hydrolase, Protease, Serine protease, Stress response, A54556A, enopeptin, depsipeptide, antibiotics, HYDROLASE-ANTIBIOTIC complex

BINDING SITE FOR CHAIN O OF ACYLDEPSIPEPTIDE 2
BINDING SITE FOR CHAIN P OF ACYLDEPSIPEPTIDE 2
BINDING SITE FOR CHAIN Q OF ACYLDEPSIPEPTIDE 2
BINDING SITE FOR CHAIN R OF ACYLDEPSIPEPTIDE 2
BINDING SITE FOR CHAIN S OF ACYLDEPSIPEPTIDE 2
BINDING SITE FOR CHAIN T OF ACYLDEPSIPEPTIDE 2
BINDING SITE FOR CHAIN U OF ACYLDEPSIPEPTIDE 2
BINDING SITE FOR CHAIN V OF ACYLDEPSIPEPTIDE 2
BINDING SITE FOR CHAIN W OF ACYLDEPSIPEPTIDE 2
BINDING SITE FOR CHAIN X OF ACYLDEPSIPEPTIDE 2
BINDING SITE FOR CHAIN Y OF ACYLDEPSIPEPTIDE 2
BINDING SITE FOR CHAIN Z OF ACYLDEPSIPEPTIDE 2
BINDING SITE FOR CHAIN 0 OF ACYLDEPSIPEPTIDE 2
BINDING SITE FOR CHAIN 1 OF ACYLDEPSIPEPTIDE 2