6UQO
ClpA/ClpP Engaged State bound to RepA-GFP
Summary for 6UQO
| Entry DOI | 10.2210/pdb6uqo/pdb |
| EMDB information | 20851 |
| Descriptor | ATP-dependent Clp protease ATP-binding subunit ClpA, ATP-dependent Clp endopeptidase proteolytic subunit ClpP, RepA-GFP, ... (5 entities in total) |
| Functional Keywords | aaa+, chaperone, protease, hsp100, atpase |
| Biological source | Escherichia coli (strain K12) More |
| Total number of polymer chains | 22 |
| Total formula weight | 693212.34 |
| Authors | Lopez, K.L.,Rizo, A.N.,Southworth, D.R. (deposition date: 2019-10-21, release date: 2020-04-22, Last modification date: 2022-03-16) |
| 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 Cited by 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: 32313240DOI: 10.1038/s41594-020-0409-5 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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