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2vb3

From Proteopedia

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[[Image:2vb3.jpg|left|200px]]
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[[Image:2vb3.png|left|200px]]
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{{STRUCTURE_2vb3| PDB=2vb3 | SCENE= }}
{{STRUCTURE_2vb3| PDB=2vb3 | SCENE= }}
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'''CRYSTAL STRUCTURE OF AG(I)CUSF'''
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===CRYSTAL STRUCTURE OF AG(I)CUSF===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 18157124 is the PubMed ID number.
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{{ABSTRACT_PUBMED_18157124}}
==About this Structure==
==About this Structure==
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[[Category: Metal-binding]]
[[Category: Metal-binding]]
[[Category: Periplasm]]
[[Category: Periplasm]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:31:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:59:39 2008''

Revision as of 14:59, 27 July 2008

Image:2vb3.png

Template:STRUCTURE 2vb3

CRYSTAL STRUCTURE OF AG(I)CUSF

Template:ABSTRACT PUBMED 18157124

About this Structure

2VB3 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 Jul 27 17:59:39 2008

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