2vb2
From Proteopedia
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'''CRYSTAL STRUCTURE OF CU(I)CUSF''' | '''CRYSTAL STRUCTURE OF CU(I)CUSF''' | ||
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[[Category: Stasser, J P.]] | [[Category: Stasser, J P.]] | ||
[[Category: Xue, Y.]] | [[Category: Xue, Y.]] | ||
| - | [[Category: | + | [[Category: Cation pi]] |
| - | [[Category: | + | [[Category: Copper]] |
| - | [[Category: | + | [[Category: Copper tolerance]] |
| - | [[Category: | + | [[Category: Copper transport]] |
| - | [[Category: | + | [[Category: Metal transport]] |
| - | [[Category: | + | [[Category: Metal-binding]] |
| - | [[Category: | + | [[Category: Periplasm]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:31:33 2008'' | |
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Revision as of 15:31, 4 May 2008
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. 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 Sun May 4 18:31:33 2008
