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Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis.

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.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Lopez KE,Rizo AN,Tse E,Lin J,Scull NW,Thwin AC,Lucius AL,Shorter J,Southworth DR

doi

10.1038/s41594-020-0409-5

subject

Has Abstract

pub_date

2020-05-01 00:00:00

pages

406-416

issue

5

eissn

1545-9993

issn

1545-9985

pii

10.1038/s41594-020-0409-5

journal_volume

27

pub_type

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