1Y7O

The structure of Streptococcus pneumoniae A153P ClpP

Summary for 1Y7O

• Entry DOI: 10.2210/pdb1y7o/pdb
• Descriptor: ATP-dependent Clp protease proteolytic subunit, CALCIUM ION (3 entities in total)
• Functional Keywords: protease, hydrolase
• Biological source: Streptococcus pneumoniae
• Total number of polymer chains: 7
• Total formula weight: 170284.73

Authors

Kimber, M.S.,Gribun, A.,Ching, R.,Sprangers, R.,Fiebig, K.M.,Houry, W.A. (deposition date: 2004-12-09, release date: 2005-02-08, Last modification date: 2023-11-15)

• Primary citation: Gribun, A.,Kimber, M.S.,Ching, R.,Sprangers, R.,Fiebig, K.M.,Houry, W.A.; The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation.; J.Biol.Chem., 280:16185-16196, 2005; PubMed: 15701650; DOI: 10.1074/jbc.M414124200

Experimental method

X-RAY DIFFRACTION (2.51 Å)