2vb2
From Proteopedia
Crystal structure of Cu(I)CusF
Structural highlights
FunctionCUSF_ECOLI Part of a cation efflux system that mediates resistance to copper and silver. Binds one copper per polypeptide.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMethionine-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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
Categories: Large Structures | Balakrishnan G | Davis AV | Focia P | O'Halloran TV | Penner-Hahn JE | Spiro TG | Staehlin BM | Stasser JP | Xue Y
