Journal
BIOMETALS
Volume 20, Issue 3-4, Pages 705-716Publisher
SPRINGER
DOI: 10.1007/s10534-006-9054-7
Keywords
copper; channel; transporter; structure; cryoEM
Categories
Funding
- NCRR NIH HHS [P42 RR-01081] Funding Source: Medline
- NIGMS NIH HHS [GM071590, GM07223] Funding Source: Medline
- NINDS NIH HHS [F31 NS045550, NS56825, NS45550] Funding Source: Medline
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Over a decade ago, genetic studies identified a family of small integral membrane proteins, commonly referred to as copper transporters (CTRs) that are both required and sufficient for cellular copper uptake in a yeast genetic complementation assay. We recently used electron crystallography to determine a projection density map of the human high affinity transporter hCTR1 embedded into a lipid bilayer. At 6 angstrom resolution, this first glimpse of the structure revealed that hCTR1 is trimeric and possesses the type of radial symmetry that traditionally has been associated with the structure of certain ion channels such as potassium or gap junction channels. Representative for this particular type of architecture, a region of low protein density at the center of the trimer is consistent with the existence of a copper permeable pore along the center three-fold axis of the trimer. In this contribution, we will briefly discuss how recent structure-function studies correlate with the projection density map, and provide a perspective with respect to the cellular uptake of other transition metals.
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