2VB2 : Crystal structure of Cu(I)CusF

  • Yi Xue (Contributor)
  • Anna V. Davis (Contributor)
  • Gurusamy Balakrishnan (Contributor)
  • Jay P. Stasser (Contributor)
  • Benjamin M. Staehlin (Contributor)
  • Pamela J Focia (Contributor)
  • T. G. Spiro (Contributor)
  • James E. Penner-Hahn (Contributor)
  • Thomas V. O'Halloran (Contributor)



Experimental Technique/Method:X-RAY DIFFRACTION
Classification:METAL TRANSPORT
Release Date:2007-12-18
Deposition Date:2007-09-06
Revision Date:2011-07-13
Molecular Weight:10025.83
Macromolecule Type:Protein
Residue Count:88
Atom Site Count:588

Methionine-rich motifs have an important role in copper trafficking factors, including the CusF protein. Here we show that CusF uses a new metal recognition site wherein Cu(I) is tetragonally displaced from a Met2His ligand plane toward a conserved tryptophan. Spectroscopic studies demonstrate that both thioether ligation and strong cation-pi interactions with tryptophan stabilize metal binding. This novel active site chemistry affords mechanisms for control of adventitious metal redox and substitution chemistry.
Date made available2007

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