6LSY

AAA+ ATPase, ClpL from Streptococcus pneumoniae - ATP bound

This is a non-PDB format compatible entry.

Summary for 6LSY

• Entry DOI: 10.2210/pdb6lsy/pdb
• EMDB information: 0965
• Descriptor: ATP-dependent Clp protease, ATP-binding subunit (1 entity in total)
• Functional Keywords: aaa+ atpase, chaperone, streptococcus pneumoniae
• Biological source: Streptococcus pneumoniae
• Total number of polymer chains: 14
• Total formula weight: 1086387.32

Authors

Kim, G.,Lee, S.G.,Han, S.,Jung, J.,Jeong, H.S.,Hyun, J.K.,Rhee, D.K.,Kim, H.M.,Lee, S. (deposition date: 2020-01-20, release date: 2021-01-27, Last modification date: 2024-03-27)

Primary citation

Kim, G.,Lee, S.G.,Han, S.,Jung, J.,Jeong, H.S.,Hyun, J.K.,Rhee, D.K.,Kim, H.M.,Lee, S.
ClpL is a functionally active tetradecameric AAA+ chaperone, distinct from hexameric/dodecameric ones.
Faseb J., 34:14353-14370, 2020

PubMed Abstract: AAA+ (ATPases associated with diverse cellular activities) chaperones are involved in a plethora of cellular activities to ensure protein homeostasis. The function of AAA+ chaperones is mostly modulated by their hexameric/dodecameric quaternary structures. Here we report the structural and biochemical characterizations of a tetradecameric AAA+ chaperone, ClpL from Streptococcus pneumoniae. ClpL exists as a tetradecamer in solution in the presence of ATP. The cryo-EM structure of ClpL at 4.5 Å resolution reveals a striking tetradecameric arrangement. Solution structures of ClpL derived from small-angle X-ray scattering data suggest that the tetradecameric ClpL could assume a spiral conformation found in active hexameric/dodecameric AAA+ chaperone structures. Vertical positioning of the middle domain accounts for the head-to-head arrangement of two heptameric rings. Biochemical activity assays with site-directed mutagenesis confirmed the critical roles of residues both in the integrity of the tetradecameric arrangement and activities of ClpL. Non-conserved Q321 and R670 are crucial in the heptameric ring assembly of ClpL. These results establish that ClpL is a functionally active tetradecamer, clearly distinct from hexameric/dodecameric AAA+ chaperones.

PubMed: 32910525
DOI: 10.1096/fj.202000843R

Experimental method

ELECTRON MICROSCOPY (6.33 Å)