AT2A1_RABIT This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction (By similarity).
Evolutionary Conservation
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Publication Abstract from PubMed
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.
Structure of a copper pump suggests a regulatory role for its metal-binding domain.,Wu CC, Rice WJ, Stokes DL Structure. 2008 Jun;16(6):976-85. PMID:18547529[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Wu CC, Rice WJ, Stokes DL. Structure of a copper pump suggests a regulatory role for its metal-binding domain. Structure. 2008 Jun;16(6):976-85. PMID:18547529 doi:http://dx.doi.org/10.1016/j.str.2008.02.025
