3MT6

Structure of ClpP from Escherichia coli in complex with ADEP1

Summary for 3MT6

• Entry DOI: 10.2210/pdb3mt6/pdb
• Related: 1TYF 1Y7O 1YG6 2FZS 3KTG 3KTH 3KTI 3KTJ 3KTK
• Related PRD ID: PRD_000503
• Descriptor: ATP-dependent Clp protease proteolytic subunit, ACYLDEPSIPEPTIDE 1, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
• Functional Keywords: endopeptidase clp, caseinolytic protease, protease ti, acypdepsipeptide antibiotics, hydrolase-antibiotic complex, hydrolase/antibiotic
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm: P0A6G7
• Total number of polymer chains: 56
• Total formula weight: 677085.71

Authors

Chung, Y.S. (deposition date: 2010-04-30, release date: 2010-11-03, Last modification date: 2023-11-22)

• Primary citation: Li, D.H.,Chung, Y.S.,Gloyd, M.,Joseph, E.,Ghirlando, R.,Wright, G.D.,Cheng, Y.Q.,Maurizi, M.R.,Guarne, A.,Ortega, J.; Acyldepsipeptide antibiotics induce the formation of a structured axial channel in ClpP: A model for the ClpX/ClpA-bound state of ClpP.; Chem.Biol., 17:959-969, 2010; PubMed: 20851345; DOI: 10.1016/j.chembiol.2010.07.008

Experimental method

X-RAY DIFFRACTION (1.901 Å)