Literature summary for 7.2.2.8 extracted from

Banci, L.; Bertini, I.; Ciofi-Baffoni, S.; D'Onofrio, M.; Gonnelli, L.; Marhuenda-Egea, F.C.; Ruiz-Duenas, F.J.
Solution structure of the N-terminal domain of a potential copper-translocating P-type ATPase from Bacillus subtilis in the apo and Cu(I) loaded states (2002), J. Mol. Biol., 317, 415-429.

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Cloned(Commentary)

Cloned (Comment)	Organism
the N-terminal region of BsCopA contains two domains constituted by amino acid residues 1 to 72 and 73 to 147, which are expressed both separately and together, in both cases only the 73-147 domain is folded and is stable both in the copper(I)-free and in the copper(I)-bound forms	Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure determination of the 73-147 domain in the 1-151 construct, in the apo state through 1H, 15N and 13C NMR spectroscopies, the structure of the Cu(I)-loaded 73-147 domain has been also determined in the construct 73-151	Bacillus subtilis

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	O32220	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the soluble domain of BsCopA has the same beta-alpha-beta-beta-alpha-beta structure as all proteins involved in the copper transport characterized so far	Bacillus subtilis	?	-	?

Synonyms

Synonyms	Comment	Organism
BsCopA	-	Bacillus subtilis
CopA	-	Bacillus subtilis

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Release 2023.1 (January 2023)