2vb2
From Proteopedia
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|PDB= 2vb2 |SIZE=350|CAPTION= <scene name='initialview01'>2vb2</scene>, resolution 1.70Å | |PDB= 2vb2 |SIZE=350|CAPTION= <scene name='initialview01'>2vb2</scene>, resolution 1.70Å | ||
|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= | + | |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.]] | ||
| - | [[Category: CU]] | ||
| - | [[Category: SO4]] | ||
[[Category: cation pi]] | [[Category: cation pi]] | ||
[[Category: copper]] | [[Category: copper]] | ||
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[[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 Mon Mar 31 05:10:34 2008'' |
Revision as of 02:10, 31 March 2008
| |||||||
| , 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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