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: 32910525; DOI: 10.1096/fj.202000843R

Experimental method

ELECTRON MICROSCOPY (6.33 Å)