Literature summary for 3.4.21.53 extracted from

Garcia-Nafria, J.; Ondrovicova, G.; Blagova, E.; Levdikov, V.M.; Bauer, J.A.; Suzuki, C.K.; Kutejova, E.; Wilkinson, A.J.; Wilson, K.S.
Structure of the catalytic domain of the human mitochondrial Lon protease: proposed relation of oligomer formation and activity (2010), Protein Sci., 19, 987-999.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of the proteolytic domain, residues 741-959, in Escherichia coli	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of the proteolytic domain of human mitochondrial Lon at 2 A resolution. There are six protomers in the asymmetric unit, four arranged as two dimers. The intersubunit interactions within the two dimers are similar to those between adjacent subunits of the hexameric ring of Escherichia coli Lon. The active site contains a 310 helix attached to the N-terminal end of alpha-helix 2, which leads to the insertion of Asp852 into the active site. Structural considerations make it likely that this conformation is proteolytically inactive. A mechanism relating the formation of Lon oligomers with a conformational shift in the active site region coupled to a movement of a loop in the oligomer interface may convert the proteolytically inactive form seen here to the active one in the Escherichia coli hexamer	Homo sapiens

Crystallization (Comment)

Organism

structure of the proteolytic domain of human mitochondrial Lon at 2 A resolution. There are six protomers in the asymmetric unit, four arranged as two dimers. The intersubunit interactions within the two dimers are similar to those between adjacent subunits of the hexameric ring of Escherichia coli Lon. The active site contains a 310 helix attached to the N-terminal end of alpha-helix 2, which leads to the insertion of Asp852 into the active site. Structural considerations make it likely that this conformation is proteolytically inactive. A mechanism relating the formation of Lon oligomers with a conformational shift in the active site region coupled to a movement of a loop in the oligomer interface may convert the proteolytically inactive form seen here to the active one in the Escherichia coli hexamer

Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	-	Homo sapiens	5739	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P36776	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Glu-Ala-Ala-Phe-4-methoxy-2-naphthylamide + H2O	-	Homo sapiens	Glu-Ala-Ala-Phe + 4-methoxy-2-naphthylamine	-	?

Subunits

Subunits	Comment	Organism
hexamer	gel filtration and glutaraldehyde crosslinking	Homo sapiens