2c9p

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[[Category: metal-binding]]
[[Category: metal-binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:03:10 2007''
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Revision as of 14:57, 30 October 2007


2c9p, resolution 2.25Å

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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 ... [(full description)]

About this Structure

2C9P is a [Single protein] structure of sequence from [Pseudomonas syringae pv. tomato] with CU and NO3 as [ligands]. Structure known Active Site: AC1. 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

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