4U9R

Structure of the N-terminal Extension from Cupriavidus metallidurans CzcP

Summary for 4U9R

• Entry DOI: 10.2210/pdb4u9r/pdb
• Descriptor: CzcP cation efflux P1-ATPase, CADMIUM ION, 3,3',3''-phosphanetriyltripropanoic acid, ... (4 entities in total)
• Functional Keywords: ferredoxin-like domain, hydrolase
• Biological source: Ralstonia metallidurans
• Cellular location: Cell membrane : Q1LAJ7
• Total number of polymer chains: 1
• Total formula weight: 23020.20

Authors

Smith, A.T.,Rosenzweig, A.C. (deposition date: 2014-08-06, release date: 2015-07-08, Last modification date: 2023-12-27)

Primary citation

Smith, A.T.,Barupala, D.,Stemmler, T.L.,Rosenzweig, A.C.
A new metal binding domain involved in cadmium, cobalt and zinc transport.
Nat.Chem.Biol., 11:678-684, 2015

PubMed 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 Cd(2+), Co(2+) or Zn(2+) 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.

PubMed: 26192600
DOI: 10.1038/nchembio.1863

Experimental method

X-RAY DIFFRACTION (2.17 Å)