6UQE

ClpA/ClpP Disengaged State bound to RepA-GFP

6UQE の概要

• エントリーDOI: 10.2210/pdb6uqe/pdb
• EMDBエントリー: 20845
• 分子名称: ATP-dependent Clp protease ATP-binding subunit ClpA, ATP-dependent Clp protease proteolytic subunit, RepA-GFP, ... (6 entities in total)
• 機能のキーワード: aaa+, chaperone, protease, hsp100, atpase
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 22
• 化学式量合計: 693467.66

構造登録者

Lopez, K.L.,Rizo, A.R.,Southworth, D.R. (登録日: 2019-10-18, 公開日: 2020-04-22, 最終更新日: 2024-12-25)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (3 Å)