1nm4
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1nm4.jpg|left|200px]] | [[Image:1nm4.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1nm4", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1nm4| PDB=1nm4 | SCENE= }} | |
| - | + | ||
| - | | | + | |
| - | }} | + | |
'''Solution structure of Cu(I)-CopC from Pseudomonas syringae''' | '''Solution structure of Cu(I)-CopC from Pseudomonas syringae''' | ||
| Line 31: | Line 28: | ||
[[Category: SPINE, Structural Proteomics in Europe.]] | [[Category: SPINE, Structural Proteomics in Europe.]] | ||
[[Category: Thompsett, A R.]] | [[Category: Thompsett, A R.]] | ||
| - | [[Category: | + | [[Category: Copper trafficking]] |
| - | [[Category: | + | [[Category: Redox switch]] |
| - | [[Category: | + | [[Category: Spine]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: | + | [[Category: Structural proteomics in europe]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:07:58 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun | + | |
Revision as of 05:07, 13 April 2008
Solution structure of Cu(I)-CopC from Pseudomonas syringae
Overview
The protein CopC from Pseudomonas syringae has been found capable of binding copper(I) and copper(II) at two different sites, occupied either one at a time or simultaneously. The protein, consisting of 102 amino acids, is known to bind copper(II) in a position that is now found consistent with a coordination arrangement including His-1, Glu-27, Asp-89, and His-91. A full solution structure analysis is reported here for Cu(I)-CopC. The copper(I) site is constituted by His-48 and three of the four Met residues (40, 43, 46, 51), which are clustered in a Met-rich region. Both copper binding sites have been characterized through extended x-ray absorption fine structure studies. They represent novel coordination environments for copper in proteins. The two sites are approximately 30 A far apart and have little affinity for the ion in the other oxidation state. Oxidation of Cu(I)-CopC or reduction of Cu(II)-CopC causes migration of copper from one site to the other. This behavior is observed both in NMR and EXAFS studies and indicates that CopC can exchange copper between two sites activated by a redox switch. CopC resides in the periplasm of Gram-negative bacteria where there is a multicopper oxidase, CopA, which may modulate the redox state of copper. CopC and CopA are coded in the same operon, responsible for copper resistance. These peculiar and novel properties of CopC are discussed with respect to their relevance for copper homeostasis.
About this Structure
1NM4 is a Single protein structure of sequence from Pseudomonas syringae. Full crystallographic information is available from OCA.
Reference
A redox switch in CopC: an intriguing copper trafficking protein that binds copper(I) and copper(II) at different sites., Arnesano F, Banci L, Bertini I, Mangani S, Thompsett AR, Proc Natl Acad Sci U S A. 2003 Apr 1;100(7):3814-9. Epub 2003 Mar 21. PMID:12651950 Page seeded by OCA on Sun Apr 13 08:07:58 2008
