6V11

Lon Protease from Yersinia pestis

Summary for 6V11

• Entry DOI: 10.2210/pdb6v11/pdb
• Related: 6ON2
• EMDB information: 21009
• Descriptor: Lon protease, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• Functional Keywords: aaa+ atpase, quality control, protease, hydrolase
• Biological source: Yersinia pestis
• Total number of polymer chains: 6
• Total formula weight: 348821.18

Authors

Shin, M.,Puchades, C.,Asmita, A.,Puri, N.,Adjei, E.,Wiseman, R.L.,Karzai, A.W.,Lander, G.C. (deposition date: 2019-11-19, release date: 2020-01-22, Last modification date: 2024-03-06)

Primary citation

Shin, M.,Puchades, C.,Asmita, A.,Puri, N.,Adjei, E.,Wiseman, R.L.,Karzai, A.W.,Lander, G.C.
Structural basis for distinct operational modes and protease activation in AAA+ protease Lon.
Sci Adv, 6:eaba8404-eaba8404, 2020

PubMed Abstract: 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.

PubMed: 32490208
DOI: 10.1126/sciadv.aba8404

Experimental method

ELECTRON MICROSCOPY (3.8 Å)