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2vb2

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|PDB= 2vb2 |SIZE=350|CAPTION= <scene name='initialview01'>2vb2</scene>, resolution 1.70&Aring;
|PDB= 2vb2 |SIZE=350|CAPTION= <scene name='initialview01'>2vb2</scene>, resolution 1.70&Aring;
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+X'>AC1</scene> and <scene name='pdbsite=AC2:Cu+Binding+Site+For+Chain+X'>AC2</scene>
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+X'>AC1</scene> and <scene name='pdbsite=AC2:Cu+Binding+Site+For+Chain+X'>AC2</scene>
-
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=CU:COPPER (II) ION'>CU</scene>
+
|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=[[1zeq|1ZEQ]], [[2vb3|2VB3]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vb2 OCA], [http://www.ebi.ac.uk/pdbsum/2vb2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2vb2 RCSB]</span>
}}
}}
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[[Category: Stasser, J P.]]
[[Category: Stasser, J P.]]
[[Category: Xue, Y.]]
[[Category: Xue, Y.]]
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[[Category: CU]]
 
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[[Category: SO4]]
 
[[Category: cation pi]]
[[Category: cation pi]]
[[Category: copper]]
[[Category: copper]]
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[[Category: periplasm]]
[[Category: periplasm]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:45:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:10:34 2008''

Revision as of 02:10, 31 March 2008


PDB ID 2vb2

Drag the structure with the mouse to rotate
, resolution 1.70Å
Sites: and
Ligands: ,
Related: 1ZEQ, 2VB3


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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