6TTY

Structure of ClpP from Staphylococcus aureus (apo, closed state)

Summary for 6TTY

• Entry DOI: 10.2210/pdb6tty/pdb
• Related: 3V5E
• Descriptor: ATP-dependent Clp protease proteolytic subunit (2 entities in total)
• Functional Keywords: caseinolytic protease, allosteric regulation, extended conformation, closed state, hydrolase
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 14
• Total formula weight: 316101.52

Authors

Malik, I.T.,Pereira, R.,Vielberg, M.-T.,Mayer, C.,Straetener, J.,Thomy, D.,Famulla, K.,Castro, H.C.,Sass, P.,Groll, M.,Broetz-Oesterheldt, H. (deposition date: 2019-12-30, release date: 2020-03-25, Last modification date: 2024-01-24)

• Primary citation: Malik, I.T.,Pereira, R.,Vielberg, M.T.,Mayer, C.,Straetener, J.,Thomy, D.,Famulla, K.,Castro, H.,Sass, P.,Groll, M.,Brotz-Oesterhelt, H.; Functional Characterisation of ClpP Mutations Conferring Resistance to Acyldepsipeptide Antibiotics in Firmicutes.; Chembiochem, 21:1997-2012, 2020; PubMed: 32181548; DOI: 10.1002/cbic.201900787

Experimental method

X-RAY DIFFRACTION (1.9 Å)