Structure and interactions of the C-terminal metal binding domain of Archaeoglobus fulgidus CopA

Journal Article · Fri Aug 13 04:00:00 EDT 2010 · Proteins

DOI:https://doi.org/10.1002/prot.22753· OSTI ID:1002594

Agarwal, S; Hong, D; Desai, N K; H Sazinsky, M; Argüello, J M; Rosenzweig, A C ^[1]

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1. NWU

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.

• Research Organization: Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
• Sponsoring Organization: USDOE
• OSTI ID: 1002594
• Journal Information: Proteins, Journal Name: Proteins Journal Issue: (11) ; 2010 Vol. 78; ISSN 0887-3585; ISSN PSFGEY
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

36 MATERIALS SCIENCE
ACTUATORS
COPPER
CRYSTAL STRUCTURE
FUNCTIONALS
HEAVY METALS
HYDROLYSIS
MEMBRANE PROTEINS
MEMBRANES
MONOMERS
NUCLEOTIDES
REGULATIONS
RESOLUTION
TRANSLOCATION
TRANSPORT