ArticleProteins2010
Structure and interactions of the C-terminal metal binding domain of Archaeoglobus fulgidus CopA.
Article in Proteins, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- The CopA2-Type PFrontiers in microbiology · 2021Article
- Transmembrane Cu(I) P-type ATPase pumps are electrogenic uniporters.Dalton transactions (Cambridge, England : 2003) · 2020Article
- Cu Homeostasis in Bacteria: The Ins and Outs.Membranes · 2020Review
- CopR, a Global Regulator of Transcription to Maintain Copper Homeostasis inFrontiers in microbiology · 2020Article
- Human copper transporter ATP7B (Wilson disease protein) forms stable dimersThe Journal of biological chemistry · 2017Article
- Assessing the genetic diversity of Cu resistance in mine tailings through high-throughput recovery of full-length copA genes.Scientific reports · 2015Article
- Role of an archaeal PitA transporter in the copper and arsenic resistance of Metallosphaera sedula, an extreme thermoacidophile.Journal of bacteriology · 2014Article
- Diversity of the metal-transporting P1B-type ATPases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- Abundance, activity, and diversity of archaeal and bacterial communities in both uncontaminated and highly copper-contaminated marine sediments.Marine biotechnology (New York, N.Y.) · 2014Article
- Metal resistance and lithoautotrophy in the extreme thermoacidophile Metallosphaera sedula.Journal of bacteriology · 2012Article
- The C-terminal domain of the virulence factor MgtC is a divergent ACT domain.Journal of bacteriology · 2012Article
- Conformations of the apo-, substrate-bound and phosphate-bound ATP-binding domain of the Cu(II) ATPase CopB illustrate coupling of domain movement to the catalytic cycle.Bioscience reports · 2012Article
- McsA and the roles of metal-binding motif in Staphylococcus aureus.FEMS microbiology letters · 2012Article
- Toward a molecular understanding of metal transport by P(1B)-type ATPases.Current topics in membranes · 2012Article
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Authors and funding
6 authors.
Funding
Abstract
The Cu(+)-ATPase CopA from Archaeoglobus fulgidus belongs to the P(1B) family of the P-type ATPases. These integral membrane proteins couple the energy of ATP hydrolysis to heavy metal ion translocation across membranes. A defining feature of P(1B-1)-type ATPases is the presence of soluble metal binding domains at the N-terminus (N-MBDs). The N-MBDs exhibit a conserved ferredoxin-like fold, similar to that of soluble copper chaperones, and bind metal ions via a conserved CXXC motif. The N-MBDs enable Cu(+) regulation of turnover rates apparently through Cu-sensitive interactions with catalytic domains. A. fulgidus CopA is unusual in that it contains both an N-terminal MBD and a C-terminal MBD (C-MBD). The functional role of the unique C-MBD has not been established. Here, we report the crystal structure of the apo, oxidized C-MBD to 2.0 A resolution. In the structure, two C-MBD monomers form a domain-swapped dimer, which has not been observed previously for similar domains. In addition, the interaction of the C-MBD with the other cytoplasmic domains of CopA, the ATP binding domain (ATPBD) and actuator domain (A-domain), has been investigated. Interestingly, the C-MBD interacts specifically with both of these domains, independent of the presence of Cu(+) or nucleotides. These data reinforce the uniqueness of the C-MBD and suggest a distinct structural role for the C-MBD in CopA transport.
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