4YPN

Crystal structure of a LonA fragment containing the 3-helix bundle and the AAA-alpha/beta domain

Summary for 4YPN

• Entry DOI: 10.2210/pdb4ypn/pdb
• Related: 4YPL 4YPM
• Descriptor: Lon protease (2 entities in total)
• Functional Keywords: aaa+ domain, helix-bundle, disordered, hydrolase
• Biological source: Meiothermus taiwanensis
• Total number of polymer chains: 1
• Total formula weight: 33571.48

Authors

Chang, C.-I.,Lin, C.-C. (deposition date: 2015-03-13, release date: 2016-03-16, Last modification date: 2023-11-08)

Primary citation

Lin, C.-C.,Su, S.-C.,Su, M.-Y.,Liang, P.-H.,Feng, C.-C.,Wu, S.-H.,Chang, C.-I.
Structural Insights into the Allosteric Operation of the Lon AAA+ Protease
Structure, 24:667-675, 2016

PubMed Abstract: The Lon AAA+ protease (LonA) is an evolutionarily conserved protease that couples the ATPase cycle into motion to drive substrate translocation and degradation. A hallmark feature shared by AAA+ proteases is the stimulation of ATPase activity by substrates. Here we report the structure of LonA bound to three ADPs, revealing the first AAA+ protease assembly where the six protomers are arranged alternately in nucleotide-free and bound states. Nucleotide binding induces large coordinated movements of conserved pore loops from two pairs of three non-adjacent protomers and shuttling of the proteolytic groove between the ATPase site and a previously unknown Arg paddle. Structural and biochemical evidence supports the roles of the substrate-bound proteolytic groove in allosteric stimulation of ATPase activity and the conserved Arg paddle in driving substrate degradation. Altogether, this work provides a molecular framework for understanding how ATP-dependent chemomechanical movements drive allosteric processes for substrate degradation in a major protein-destruction machine.

PubMed: 27041592
DOI: 10.1016/j.str.2016.03.001

Experimental method

X-RAY DIFFRACTION (2.07 Å)