2vb3: Difference between revisions
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[[Image:2vb3.jpg|left|200px]] | [[Image:2vb3.jpg|left|200px]] | ||
'''CRYSTAL STRUCTURE OF AG(I)CUSF''' | {{Structure | ||
|PDB= 2vb3 |SIZE=350|CAPTION= <scene name='initialview01'>2vb3</scene>, resolution 2.33Å | |||
|SITE= <scene name='pdbsite=AC1:Ag+Binding+Site+For+Chain+X'>AC1</scene> | |||
|LIGAND= <scene name='pdbligand=AG:SILVER ION'>AG</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF AG(I)CUSF''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2VB3 is a [ | 2VB3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VB3 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/18157124 18157124] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: periplasm]] | [[Category: periplasm]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:45:04 2008'' | ||
Revision as of 16:45, 20 March 2008
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| 2vb3, resolution 2.33Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | AG | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE OF AG(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
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
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