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-Structure paper
タイトル | Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 27, Issue 5, Page 406-416, Year 2020 |
掲載日 | 2020年4月20日 |
![]() | Kyle E Lopez / Alexandrea N Rizo / Eric Tse / JiaBei Lin / Nathaniel W Scull / Aye C Thwin / Aaron L Lucius / James Shorter / Daniel R Southworth / ![]() |
PubMed 要旨 | 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 ...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. |
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手法 | EM (単粒子) |
解像度 | 2.7 - 3.4 Å |
構造データ | EMDB-20845, PDB-6uqe: EMDB-20851, PDB-6uqo: EMDB-21519, PDB-6w1z: EMDB-21520, PDB-6w20: EMDB-21521, PDB-6w21: EMDB-21522, PDB-6w22: EMDB-21523, PDB-6w23: EMDB-21524, PDB-6w24: |
化合物 | ![]() ChemComp-ADP: ![]() ChemComp-AGS: ![]() ChemComp-ATP: |
由来 |
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![]() | CHAPERONE / AAA+ / Protease / Hsp100 / ATPase |