2vb3
From Proteopedia
(New page: 200px<br /><applet load="2vb3" size="350" color="white" frame="true" align="right" spinBox="true" caption="2vb3, resolution 2.33Å" /> '''CRYSTAL STRUCTURE OF...) |
|||
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | Methionine-rich motifs have an important role in copper trafficking | + | 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== | ==About this Structure== | ||
| - | 2VB3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=AG:'>AG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Ag Binding Site For Chain X'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VB3 OCA]. | + | 2VB3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=AG:'>AG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Ag+Binding+Site+For+Chain+X'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VB3 OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Balakrishnan, G.]] | [[Category: Balakrishnan, G.]] | ||
| - | [[Category: Davis, A | + | [[Category: Davis, A V.]] |
[[Category: Focia, P.]] | [[Category: Focia, P.]] | ||
| - | [[Category: Halloran, T | + | [[Category: Halloran, T V.O.]] |
| - | [[Category: Penner-Hahn, J | + | [[Category: Penner-Hahn, J E.]] |
| - | [[Category: Spiro, T | + | [[Category: Spiro, T G.]] |
| - | [[Category: Staehlin, B | + | [[Category: Staehlin, B M.]] |
| - | [[Category: Stasser, J | + | [[Category: Stasser, J P.]] |
[[Category: Xue, Y.]] | [[Category: Xue, Y.]] | ||
[[Category: AG]] | [[Category: AG]] | ||
| Line 31: | Line 31: | ||
[[Category: periplasm]] | [[Category: periplasm]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:54:44 2008'' |
Revision as of 16:54, 21 February 2008
|
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 with as ligand. Known structural/functional Site: . 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 Thu Feb 21 18:54:44 2008
