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-Structure paper
タイトル | Structural basis for distinct operational modes and protease activation in AAA+ protease Lon. |
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ジャーナル・号・ページ | Sci Adv, Vol. 6, Issue 21, Page eaba8404, Year 2020 |
掲載日 | 2020年5月20日 |
![]() | Mia Shin / Cristina Puchades / Ananya Asmita / Neha Puri / Eric Adjei / R Luke Wiseman / A Wali Karzai / Gabriel C Lander / ![]() |
PubMed 要旨 | Substrate-bound structures of AAA+ protein translocases reveal a conserved asymmetric spiral staircase architecture wherein a sequential ATP hydrolysis cycle drives hand-over-hand substrate ...Substrate-bound structures of AAA+ protein translocases reveal a conserved asymmetric spiral staircase architecture wherein a sequential ATP hydrolysis cycle drives hand-over-hand substrate translocation. However, this configuration is unlikely to represent the full conformational landscape of these enzymes, as biochemical studies suggest distinct conformational states depending on the presence or absence of substrate. Here, we used cryo-electron microscopy to determine structures of the Lon AAA+ protease in the absence and presence of substrate, uncovering the mechanistic basis for two distinct operational modes. In the absence of substrate, Lon adopts a left-handed, "open" spiral organization with autoinhibited proteolytic active sites. Upon the addition of substrate, Lon undergoes a reorganization to assemble an enzymatically active, right-handed "closed" conformer with active protease sites. These findings define the mechanistic principles underlying the operational plasticity required for processing diverse protein substrates. |
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手法 | EM (単粒子) |
解像度 | 3.0 - 3.8 Å |
構造データ | EMDB-20133, PDB-6on2: EMDB-21009, PDB-6v11: |
化合物 | ![]() ChemComp-ATP: ![]() ChemComp-MG: ![]() ChemComp-ADP: |
由来 |
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![]() | HYDROLASE / Lon / mitochondrial protease / AAA+ / ATPase / AAA+ ATPase / Quality Control / Protease |