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Literature summary for 7.2.2.8 extracted from

  • Zhou, L.; Singleton, C.; Le Brun, N.E.
    CopAb, the second N-terminal soluble domain of Bacillus subtilis CopA, dominates the Cu(I)-binding properties of CopAab (2012), Dalton Trans., 41, 5939-5948.
    View publication on PubMed
Search for more literature for 7.2.2.8

Cloned(Commentary)

Cloned (Comment) Organism
gene copAab, expression of full-length enzyme and N-terminal domains CopAa and CopAb in Escherichia coli strain BL21(DE3) Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + Cu+[side 1] Bacillus subtilis
-
 ADP + phosphate + Cu+[side 2]
-
 ?
ATP + H2O + Cu+[side 1] Bacillus subtilis 168
-
 ADP + phosphate + Cu+[side 2]
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis O32220
-
-
Bacillus subtilis 168 O32220
-
-

Purification (Commentary)

Purification (Comment) Organism
gene copAab, recombinant full-length enzyme and N-terminal domains CopAa and CopAb from Escherichia coli strain BL21(DE3) by anion exchange chromatography, ultrafiltration, and gel filtration Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Cu+[side 1]
-
 Bacillus subtilis ADP + phosphate + Cu+[side 2]
-
 ?
ATP + H2O + Cu+[side 1]
-
 Bacillus subtilis 168 ADP + phosphate + Cu+[side 2]
-
 ?

Subunits

Subunits Comment Organism
? x * 8256.44, recombinant N-terminal domain CopAb, mass spectrometry, x * 8258.17, N-terminal domain CopAb, sequence calculation Bacillus subtilis

Synonyms

Synonyms Comment Organism
CopA
-
 Bacillus subtilis
Cu(I)-detoxifying P-type ATPase
-
 Bacillus subtilis
Cu(I)-transporting P-type ATPase
-
 Bacillus subtilis

General Information

General Information Comment Organism
additional information the enzyme CopA contains two N-terminal soluble domains, CopAa and CopAb, connected by a short linker, both domains are able to bind Cu(I) extremely tightly. Isolated N-terminal soluble domains CopAa and CopAb bind Cu(I) with an extremely high affinity and remain as a monomers up to a level of 1 Cu(I) per protein. Above this level, they undergo dimerization. The Cu(I)-binding properties of CopAb are very similar to those of the two-domain protein CopAab, indicating that this domain plays a dominant role in determining the binding properties of CopAab. The MTCAAC Cu(I)-binding motif of each domain is located at opposite ends of the protein molecule, ruling out the possibility of intra protein, inter-domain Cu(I)-binding, proposed model of Cu(I)-binding to CopAb and the resulting association state changes, overview. CopAb in isolation does not undergo Cu(I)-mediated unfolding, the unfolding of CopAab at high levels of Cu(I) is due to the instability of the CopAa domain and the remaining secondary structure observed at high Cu(I) levels in CopAab is due to the stable CopAb domain Bacillus subtilis
physiological function the P-type ATPase CopA plays a major role in the resistance of the cell to copper. The N-terminal domains of Cu(I)-transporting P-type ATPases interact with other domains of the transporter, thereby regulating transport activity Bacillus subtilis