A new metal binding domain involved in cadmium, cobalt and zinc transport

Aaron T. Smith, Dulmini Barupala, Timothy L. Stemmler, Amy C. Rosenzweig*

*Corresponding author for this work

Research output: Contribution to journalArticle

14 Scopus citations

Abstract

The P1B-ATPases, which couple cation transport across membranes to ATP hydrolysis, are central to metal homeostasis in all organisms. An important feature of P1B-ATPases is the presence of soluble metal binding domains (MBDs) that regulate transport activity. Only one type of MBD has been characterized extensively, but bioinformatics analyses indicate that a diversity of MBDs may exist in nature. Here we report the biochemical, structural and functional characterization of a new MBD from the Cupriavidus metallidurans P1B-4 -ATPase CzcP (CzcP MBD). The CzcP MBD binds two Cd2+, Co2+ or Zn2+ ions in distinct and unique sites and adopts an unexpected fold consisting of two fused ferredoxin-like domains. Both in vitro and in vivo activity assays using full-length CzcP, truncated CzcP and several variants indicate a regulatory role for the MBD and distinct functions for the two metal binding sites. Taken together, these findings elucidate a previously unknown MBD and suggest new regulatory mechanisms for metal transport by P1B-ATPases.

Original languageEnglish (US)
Pages (from-to)678-684
Number of pages7
JournalNature Chemical Biology
Volume11
Issue number9
DOIs
StatePublished - Sep 20 2015

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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