2vb2
From Proteopedia
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CRYSTAL STRUCTURE OF CU(I)CUSF
Overview
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.
About this Structure
2VB2 is a Single protein structure of sequence from Escherichia coli with and as ligands. Known structural/functional Sites: and . Full crystallographic information is available from OCA.
Reference
Cu(I) recognition via cation-pi and methionine interactions in CusF., Xue Y, Davis AV, Balakrishnan G, Stasser JP, Staehlin BM, Focia P, Spiro TG, Penner-Hahn JE, O'Halloran TV, Nat Chem Biol. 2008 Feb;4(2):107-9. Epub 2007 Dec 23. PMID:18157124
Page seeded by OCA on Wed Jan 23 11:13:50 2008
Categories: Escherichia coli | Single protein | Balakrishnan, G. | Davis, A.V. | Focia, P. | Halloran, T.V.O. | Penner-Hahn, J.E. | Spiro, T.G. | Staehlin, B.M. | Stasser, J.P. | Xue, Y. | CU | SO4 | Cation pi | Copper | Copper tolerance | Copper transport | Metal transport | Metal-binding | Periplasm