Journal
STRUCTURE
Volume 16, Issue 6, Pages 976-985Publisher
CELL PRESS
DOI: 10.1016/j.str.2008.02.025
Keywords
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Funding
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM056960] Funding Source: NIH RePORTER
- NIGMS NIH HHS [GM 56960, R01 GM056960, R01 GM056960-07, R01 GM056960-10, R01 GM056960-11, R01 GM056960-11S1, R01 GM056960-08, R01 GM056960-12] Funding Source: Medline
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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.
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