1FVQ

SOLUTION STRUCTURE OF THE YEAST COPPER TRANSPORTER DOMAIN CCC2A IN THE APO AND CU(I) LOADED STATES

Summary for 1FVQ

• Entry DOI: 10.2210/pdb1fvq/pdb
• Related: 1FVS
• Descriptor: COPPER-TRANSPORTING ATPASE (1 entity in total)
• Functional Keywords: apo-ccc2a, hydrolase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein: P38995
• Total number of polymer chains: 1
• Total formula weight: 7889.92

Authors

Banci, L.,Bertini, I.,Ciofi Baffoni, S.,Huffman, D.L.,O'Halloran, T.V. (deposition date: 2000-09-20, release date: 2001-03-14, Last modification date: 2024-05-22)

Primary citation

Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Huffman, D.L.,O'Halloran, T.V.
Solution structure of the yeast copper transporter domain Ccc2a in the apo and Cu(I)-loaded states.
J.Biol.Chem., 276:8415-8426, 2001

PubMed Abstract: Ccc2 is an intracellular copper transporter in Saccharomyces cerevisiae and is a physiological target of the copper chaperone Atx1. Here we describe the solution structure of the first N-terminal MTCXXC metal-binding domain, Ccc2a, both in the presence and absence of Cu(I). For Cu(I)-Ccc2a, 1944 meaningful nuclear Overhauser effects were used to obtain a family of 35 structures with root mean square deviation to the average structure of 0.36 +/- 0.06 A for the backbone and 0.79 +/- 0.05 A for the heavy atoms. For apo-Ccc2a, 1970 meaningful nuclear Overhauser effects have been used with 35 (3)J(HNHalpha) to obtain a family of 35 structures with root mean square deviation to the average structure of 0.38 +/- 0.06 A for the backbone and 0.82 +/- 0.07 A for the heavy atoms. The protein exhibits a betaalphabetabetaalphabeta, ferrodoxin-like fold similar to that of its target Atx1 and that of a human counterpart, the fourth metal-binding domain of the Menkes protein. The overall fold remains unchanged upon copper loading, but the copper-binding site itself becomes less disordered. The helical context of the copper-binding site, and the copper-induced conformational changes in Ccc2a differ from those in Atx1. Ccc2a presents a conserved acidic surface which complements the basic surface of Atx1 and a hydrophobic surface. These results open new mechanistic aspects of copper transporter domains with physiological copper donor and acceptor proteins.

PubMed: 11083871
DOI: 10.1074/jbc.M008389200

Experimental method

SOLUTION NMR