2vb3

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[[Image:2vb3.jpg|left|200px]]
[[Image:2vb3.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2vb3 |SIZE=350|CAPTION= <scene name='initialview01'>2vb3</scene>, resolution 2.33&Aring;
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The line below this paragraph, containing "STRUCTURE_2vb3", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Ag+Binding+Site+For+Chain+X'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=AG:SILVER+ION'>AG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_2vb3| PDB=2vb3 | SCENE= }}
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|RELATEDENTRY=[[1zeq|1ZEQ]], [[2vb2|2VB2]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vb3 OCA], [http://www.ebi.ac.uk/pdbsum/2vb3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2vb3 RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF AG(I)CUSF'''
'''CRYSTAL STRUCTURE OF AG(I)CUSF'''
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[[Category: Stasser, J P.]]
[[Category: Stasser, J P.]]
[[Category: Xue, Y.]]
[[Category: Xue, Y.]]
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[[Category: cation pi]]
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[[Category: Cation pi]]
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[[Category: copper]]
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[[Category: Copper]]
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[[Category: copper tolerance]]
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[[Category: Copper tolerance]]
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[[Category: copper transport]]
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[[Category: Copper transport]]
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[[Category: metal transport]]
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[[Category: Metal transport]]
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[[Category: metal-binding]]
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[[Category: Metal-binding]]
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[[Category: periplasm]]
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[[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 Mon Mar 31 05:10:33 2008''
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Revision as of 15:31, 4 May 2008

Image:2vb3.jpg

Template:STRUCTURE 2vb3

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 Page seeded by OCA on Sun May 4 18:31:46 2008

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