Structural biology of copper trafficking

Amie K. Boal, Amy C. Rosenzweig

Research output: Contribution to journalArticle

259 Scopus citations

Abstract

A study was conducted to demonstrate crystallographic, solution, and cryoelectron microscopic structures of copper chaperones and membrane-bound copper transporters for all living systems. It was demonstrated that copper transported into eukaryotic cells as Cu(I) by members of the Ctr copper transporter family. These membrane transporters were identified in yeast, plants, humans, and other animals and contained several methionine-rich motifs at their N-termini and conserved cysteine and histidine residues at their C-termini. The Cu(I) transporting PIB-type ATPases consisted of eight transmembrane (TM) helices and cytoplasmic ATP binding (ATPBD). It was also found that the Cu(I) transporting PIB-type ATPases were found in large numbers in prokaryotes.

Original languageEnglish (US)
Pages (from-to)4760-4779
Number of pages20
JournalChemical Reviews
Volume109
Issue number10
DOIs
StatePublished - Oct 14 2009

ASJC Scopus subject areas

  • Chemistry(all)

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