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• W2019958839 startingPage "976" @default.
• W2019958839 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 PIB 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." @default.
• W2019958839 created "2016-06-24" @default.
• W2019958839 creator A5022046425 @default.
• W2019958839 creator A5055849155 @default.
• W2019958839 creator A5087642015 @default.
• W2019958839 date "2008-06-01" @default.
• W2019958839 modified "2023-10-16" @default.
• W2019958839 title "Structure of a Copper Pump Suggests a Regulatory Role for Its Metal-Binding Domain" @default.
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• W2019958839 doi "https://doi.org/10.1016/j.str.2008.02.025" @default.
• W2019958839 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2705936" @default.
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