Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.7
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
DOI:10.2210/pdb2vb2/pdb
Abstract:
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.
Resolution:1.7
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
DOI:10.2210/pdb2vb2/pdb
Abstract:
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 available | 2007 |
---|---|
Publisher | RCSB-PDB |