1CC8 : CRYSTAL STRUCTURE OF THE ATX1 METALLOCHAPERONE PROTEIN

  • David L. Huffman (Contributor)
  • Amy C Rosenzweig (Contributor)
  • Amy K. Wernimont (Contributor)

Dataset

Description

Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.02
Classification:METAL TRANSPORT
Release Date:1999-12-12
Deposition Date:1999-03-04
Revision Date:2008-04-26#2011-07-13#2017-10-04
Molecular Weight:8673.54
Macromolecule Type:Protein
Residue Count:73
Atom Site Count:586
DOI:10.2210/pdb1cc8/pdb

Abstract:
Metallochaperone proteins function in the trafficking and delivery of essential, yet potentially toxic, metal ions to distinct locations and particular proteins in eukaryotic cells. The Atx1 protein shuttles copper to the transport ATPase Ccc2 in yeast cells. Molecular mechanisms for copper delivery by Atx1 and similar human chaperones have been proposed, but detailed structural characterization is necessary to elucidate how Atx1 binds metal ions and how it might interact with Ccc2 to facilitate metal ion transfer.
Date made available1999
PublisherRCSB-PDB

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