6W23

ClpA Disengaged State bound to RepA-GFP (Focused Classification)

Summary for 6W23

• Entry DOI: 10.2210/pdb6w23/pdb
• EMDB information: 21523
• Descriptor: ATP-dependent Clp protease ATP-binding subunit ClpA, RepA, green fluorescent protein fusion, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: aaa+, chaperone, protease, hsp100, atpase
• Biological source: Escherichia coli (strain K12); More
• Total number of polymer chains: 7
• Total formula weight: 513330.65

Authors

Lopez, K.L.,Rizo, A.N.,Tse, E.,Lin, J.,Scull, N.W.,Thwin, A.C.,Lucius, A.L.,Shorter, J.,Southworth, D.R. (deposition date: 2020-03-04, release date: 2020-05-06, Last modification date: 2024-03-06)

Primary citation

Lopez, K.E.,Rizo, A.N.,Tse, E.,Lin, J.,Scull, N.W.,Thwin, A.C.,Lucius, A.L.,Shorter, J.,Southworth, D.R.
Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis.
Nat.Struct.Mol.Biol., 27:406-416, 2020

PubMed Abstract: The ClpAP complex is a conserved bacterial protease that unfolds and degrades proteins targeted for destruction. The ClpA double-ring hexamer powers substrate unfolding and translocation into the ClpP proteolytic chamber. Here, we determined high-resolution structures of wild-type Escherichia coli ClpAP undergoing active substrate unfolding and proteolysis. A spiral of pore loop-substrate contacts spans both ClpA AAA+ domains. Protomers at the spiral seam undergo nucleotide-specific rearrangements, supporting substrate translocation. IGL loops extend flexibly to bind the planar, heptameric ClpP surface with the empty, symmetry-mismatched IGL pocket maintained at the seam. Three different structures identify a binding-pocket switch by the IGL loop of the lowest positioned protomer, involving release and re-engagement with the clockwise pocket. This switch is coupled to a ClpA rotation and a network of conformational changes across the seam, suggesting that ClpA can rotate around the ClpP apical surface during processive steps of translocation and proteolysis.

PubMed: 32313240
DOI: 10.1038/s41594-020-0409-5

Experimental method

ELECTRON MICROSCOPY (3.1 Å)