3FRY

Crystal structure of the CopA C-terminal metal binding domain

Summary for 3FRY

• Entry DOI: 10.2210/pdb3fry/pdb
• Descriptor: Probable copper-exporting P-type ATPase A, CITRIC ACID (3 entities in total)
• Functional Keywords: transport protein, metal binding domain, domain swap, atp-binding, cell membrane, copper transport, hydrolase, ion transport, magnesium, membrane, metal-binding, nucleotide-binding, phosphoprotein, transmembrane, transport
• Biological source: Archaeoglobus fulgidus
• Cellular location: Cell membrane; Multi-pass membrane protein: O29777
• Total number of polymer chains: 2
• Total formula weight: 15843.93

Authors

Agarwal, S.,Sazinsky, M.,Arguello, J.,Rosenzweig, A.C. (deposition date: 2009-01-08, release date: 2010-01-12, Last modification date: 2024-10-16)

Primary citation

Agarwal, S.,Hong, D.,Desai, N.K.,Sazinsky, M.H.,Arguello, J.M.,Rosenzweig, A.C.
Structure and interactions of the C-terminal metal binding domain of Archaeoglobus fulgidus CopA.
Proteins, 78:2450-2458, 2010

PubMed 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.

PubMed: 20602459
DOI: 10.1002/prot.22753

Experimental method

X-RAY DIFFRACTION (2 Å)