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TitleStructural basis for distinct operational modes and protease activation in AAA+ protease Lon.
Journal, issue, pagesSci Adv, Vol. 6, Issue 21, Page eaba8404, Year 2020
Publish dateMay 20, 2020
AuthorsMia Shin / Cristina Puchades / Ananya Asmita / Neha Puri / Eric Adjei / R Luke Wiseman / A Wali Karzai / Gabriel C Lander /
PubMed AbstractSubstrate-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.
External linksSci Adv / PubMed:32490208 / PubMed Central
MethodsEM (single particle)
Resolution3.0 - 3.8 Å
Structure data

20133

6on2

EMDB-20133, PDB-6on2:
Lon Protease from Yersinia pestis with Y2853 substrate
Method: EM (single particle) / Resolution: 3.0 Å

21009

6v11

EMDB-21009, PDB-6v11:
Lon Protease from Yersinia pestis
Method: EM (single particle) / Resolution: 3.8 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • yersinia pestis (bacteria)
KeywordsHYDROLASE / Lon / mitochondrial protease / AAA+ / ATPase / AAA+ ATPase / Quality Control / Protease

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