Literature summary for 3.4.21.53 extracted from

Li, M.; Gustchina, A.; Rasulova, F.S.; Melnikov, E.E.; Maurizi, M.R.; Rotanova, T.V.; Dauter, Z.; Wlodawer, A.
Structure of the N-terminal fragment of Escherichia coli Lon protease (2010), Acta Crystallogr. Sect. D, 66, 865-873.

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Cloned(Commentary)

Cloned (Comment)	Organism
N-terminal residues 1-245, expression in Escherichia coli	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
N-terminal residues 1-245 comprising most of the N-terminal domain of the enzyme, as selenomethionine derivative to 2.6 A resolution. The molecule consists of two compact subdomains and a very long C-terminal alpha-helix. The structure of the first subdomain, residues 1-117, which consists mostly of beta-strands, is similar to that of the shorter fragment, whereas the second subdomain is almost entirely helical. The fold and spatial relationship of the two subdomains, with the exception of the C-terminal helix, closely resemble the structure of BPP1347, a 203-amino-acid protein of unknown function from Bordetella parapertussis	Escherichia coli

Crystallization (Comment)

Organism

N-terminal residues 1-245 comprising most of the N-terminal domain of the enzyme, as selenomethionine derivative to 2.6 A resolution. The molecule consists of two compact subdomains and a very long C-terminal alpha-helix. The structure of the first subdomain, residues 1-117, which consists mostly of beta-strands, is similar to that of the shorter fragment, whereas the second subdomain is almost entirely helical. The fold and spatial relationship of the two subdomains, with the exception of the C-terminal helix, closely resemble the structure of BPP1347, a 203-amino-acid protein of unknown function from Bordetella parapertussis

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A9M0	-	-

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Release 2023.1 (January 2023)