2001
DOI: 10.1042/0264-6021:3570217
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Structure‒function analysis of purified Enterococcus hirae CopB copper ATPase: effect of Menkes/Wilson disease mutation homologues

Abstract: The Enterococcus hirae CopB ATPase (EC 3.6.1.3) confers copper resistance to the organism by expelling excess copper. Two related human ATPase genes, ATP7A (EC 3.6.1.36) and ATP7B (EC 3.6.1.36), have been cloned as the loci of mutations causing Menkes and Wilson diseases, diseases of copper metabolism. Many mutations in these genes have been identified in patients. Since it has not yet been possible to purify the human copper ATPases, it has proved difficult to test the impact of mutations on ATPase function. … Show more

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Cited by 33 publications
(12 citation statements)
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“…Replacement of either cysteine with alanine in the E. coli ZntA CPC motif also results in inactive enzyme, but ZntA variants in which the cysteines are replaced with histidine retain some activity (27). For the E. hirae CopB Cu 2+ -ATPase, alteration of the CPH transmembrane motif to SPH abolished the ability to restore copper resistance in a CopB knockout mutant in vivo, suggesting impaired Cu 2+ transport (55). …”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…Replacement of either cysteine with alanine in the E. coli ZntA CPC motif also results in inactive enzyme, but ZntA variants in which the cysteines are replaced with histidine retain some activity (27). For the E. hirae CopB Cu 2+ -ATPase, alteration of the CPH transmembrane motif to SPH abolished the ability to restore copper resistance in a CopB knockout mutant in vivo, suggesting impaired Cu 2+ transport (55). …”
Section: Resultsmentioning
confidence: 99%
“…Surprisingly, the data indicate that the cysteine residue in the conserved SPC transmembrane metal binding motif is not directly involved in Co 2+ binding in this state of the enzyme. In several P 1B -ATPases that contain cysteines in this motif (vide supra), such as E. coli CopA, A. fulgidus CopA, E. hirae CopB, and E. coli ZntA, the transmembrane cysteines appear to play essential and equivalent roles in the catalytic cycle (2527, 55). However, in other P 1B -ATPases, the cysteine residues in this motif are believed to be nonequivalent and function at different stages of the transport mechanism.…”
Section: Resultsmentioning
confidence: 99%
“…However, CopA and related ATPases are distinct from NaK-or Ca-ATPases in several regards: (1) they possess one to six N-terminal metal binding modules with a CxxC motif, (2) they feature two additional transmembrane helices at the N-terminal side and lack four at the C terminus, (3) they contain a conserved HP motif in the second large cytoplasmic domain, and (4) they contain a conserved CPC or CPH motif, involving the conserved proline mentioned above, in membrane helix six. This motif has been proposed to form the membrane-located ion binding site (Bissig et al 2001). Due to the CPx-feature, these ATPases are referred to as 'CPx-type' ATPases, but they have also been classified as P1B-type ATPases (Solioz and Vulpe 1996;Lutsenko and Kaplan 1995).…”
mentioning
confidence: 99%
“…The ATPase activity of the CopB copper ATPase is tightly linked to copper transport, and thus serves as a measure of transport activity that can effectively be determined on the solubilized enzyme as well as on the enzyme reconstituted into membrane vesicles [ 31 ]. Since CopB naturally possesses a very histidine-rich N-terminal domain, it can be purified by Ni-NTA affinity chromatography without a need to modify the protein [ 43 ].…”
Section: Resultsmentioning
confidence: 99%
“…hirae [ 30 ]. The copper pumping activity by CopB is directly linked to ATP hydrolysis: if no copper ions are available for transport, no ATP hydrolysis takes place [ 31 ]. This allows the recording of CopB activity not only in a membrane environment, but also in a solubilized state in the absence of phospholipids by monitoring ATP hydrolysis.…”
Section: Introductionmentioning
confidence: 99%