2c9p
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2c9p.gif|left|200px]]<br /> | + | [[Image:2c9p.gif|left|200px]]<br /><applet load="2c9p" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2c9p" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="2c9p, resolution 2.25Å" /> | caption="2c9p, resolution 2.25Å" /> | ||
'''CU(I)CU(II)-COPC AT PH 4.5'''<br /> | '''CU(I)CU(II)-COPC AT PH 4.5'''<br /> | ||
| Line 8: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2C9P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_syringae_pv._tomato Pseudomonas syringae pv. tomato] with CU and NO3 as [http://en.wikipedia.org/wiki/ligands ligands]. | + | 2C9P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_syringae_pv._tomato Pseudomonas syringae pv. tomato] with CU and NO3 as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:No3 Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C9P OCA]. |
==Reference== | ==Reference== | ||
| Line 27: | Line 26: | ||
[[Category: metal-binding]] | [[Category: metal-binding]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 19:15:23 2007'' |
Revision as of 17:05, 18 December 2007
|
CU(I)CU(II)-COPC AT PH 4.5
Overview
CopC is a small soluble protein expressed in the periplasm of Pseudomonas, syringae pathovar tomato as part of its copper resistance response (cop, operon). Equilibrium competition reactions confirmed two separated binding, sites with high affinities for Cu(I) (10(-7) > or = K(D) > or = 10(-13) M), and Cu(II) (K(D) = 10(-13(1)) M), respectively. While Cu(I)-CopC was, converted cleanly by O2 to Cu(II)-CopC, the fully loaded form, Cu(I)Cu(II)-CopC was stable in air. Variant forms H1F and H91F exhibited a, lower affinity for Cu(II) than does the wild-type protein while variant, E27G exhibited a higher affinity. Cation exchange chromatography detected, each of the four different types of intermolecular copper transfer, reactions possible between wild type and variant forms: Cu(I) site to, Cu(II) site; Cu(II) site to Cu(I) site; Cu(I) site to Cu(I) site; Cu(II), site to Cu(II) site. The availability of an unoccupied site of higher, affinity induced intermolecular transfer of either Cu(I) or Cu(II) in the, presence of O2 while buffering concentrations of cupric ion at, sub-picomolar levels. Crystal structures of two crystal forms of wild-type, Cu(I)Cu(II)-CopC and of the apo-H91F variant demonstrate that the core, structures of the molecules in the three crystal forms are conserved., However, the conformations of the amino terminus (a Cu(II) ligand) and the, two copper-binding loops (at each end of the molecule) differ, significantly, providing the structural lability needed to allow transfer, of copper between partners, with or without change of oxidation state., CopC has the potential to interact directly with each of the four cop, proteins coexpressed to the periplasm.
About this Structure
2C9P is a Single protein structure of sequence from Pseudomonas syringae pv. tomato with CU and NO3 as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Intermolecular transfer of copper ions from the CopC protein of Pseudomonas syringae. Crystal structures of fully loaded Cu(I)Cu(II) forms., Zhang L, Koay M, Maher MJ, Xiao Z, Wedd AG, J Am Chem Soc. 2006 May 3;128(17):5834-50. PMID:16637653
Page seeded by OCA on Tue Dec 18 19:15:23 2007
