Literature summary for 3.4.21.53 extracted from

Cha, S.S.; An, Y.J.; Lee, C.R.; Lee, H.S.; Kim, Y.G.; Kim, S.J.; Kwon, K.K.; De Donatis, G.M.; Lee, J.H.; Maurizi, M.R.; Kang, S.G.
Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber (2010), EMBO J., 29, 3520-3530.

Search for more literature for 3.4.21.53

Cloned(Commentary)

Cloned (Comment)	Organism
expression of a deletion mutant lacking the putative membrane-anchoring region, residues 134-170	Thermococcus onnurineus

Crystallization (Commentary)

Crystallization (Comment)	Organism
deletion mutant lacking the putative membrane-anchoring region, residues 134-170, and introduction of mutations S523A and K566A, to 2.0 A resolution. The structure is a three-tiered hexagonal cylinder with a large sequestered chamber accessible through an axial channel. Conserved loops extending from the ATPase domain combine with an insertion domain containing the membrane anchor to form an apical domain that serves as a gate governing substrate access to an internal unfolding and degradation chamber. Alternating ATPase domains are in tight- and weak-binding nucleotide states with different domain orientations and intersubunit contacts	Thermococcus onnurineus

Crystallization (Comment)

Organism

deletion mutant lacking the putative membrane-anchoring region, residues 134-170, and introduction of mutations S523A and K566A, to 2.0 A resolution. The structure is a three-tiered hexagonal cylinder with a large sequestered chamber accessible through an axial channel. Conserved loops extending from the ATPase domain combine with an insertion domain containing the membrane anchor to form an apical domain that serves as a gate governing substrate access to an internal unfolding and degradation chamber. Alternating ATPase domains are in tight- and weak-binding nucleotide states with different domain orientations and intersubunit contacts

Thermococcus onnurineus

Protein Variants

Protein Variants	Comment	Organism
additional information	deletion mutant lacking the putative membrane-anchoring region, residues 134-170, and introduction of mutations S523A and K566A to avoid self-degrading activity. Mutant is active for peptide cleavage and both ATP-dependent and -independent protein degradation	Thermococcus onnurineus

Organism

Organism	UniProt	Comment	Textmining
Thermococcus onnurineus	B6YU74	-	-

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Release 2023.1 (January 2023)