Format

Send to

Choose Destination
Structure. 2008 Jun;16(6):976-85. doi: 10.1016/j.str.2008.02.025.

Structure of a copper pump suggests a regulatory role for its metal-binding domain.

Author information

1
Skirball Institute of Biomolecular Medicine, School of Medicine, New York University, 540 First Avenue, New York, NY 10016, USA.

Abstract

P-type ATPases play an important role in Cu homeostasis, which provides sufficient Cu for metalloenzyme biosynthesis but prevents oxidative damage of free Cu to the cell. The P(IB) group of P-type ATPases includes ATP-dependent pumps of Cu and other transition metal ions, and it is distinguished from other family members by the presence of N-terminal metal-binding domains (MBD). We have determined structures of two constructs of a Cu pump from Archaeoglobus fulgidus (CopA) by cryoelectron microscopy of tubular crystals, which reveal the overall architecture and domain organization of the molecule. By comparing these structures, we localized its N-terminal MBD within the cytoplasmic domains that use ATP hydrolysis to drive the transport cycle. We have built a pseudoatomic model by fitting existing crystallographic structures into the cryoelectron microscopy maps for CopA, which suggest a Cu-dependent regulatory role for the MBD.

Comment in

PMID:
18547529
PMCID:
PMC2705936
DOI:
10.1016/j.str.2008.02.025
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Elsevier Science Icon for PubMed Central
Loading ...
Support Center