2opc
From Proteopedia
|
Structure of Melampsora lini avirulence protein, AvrL567-A
Overview
Metal-binding sites are ubiquitous in proteins and can be readily utilized, for phasing. It is shown that a protein crystal structure can be solved, using single-wavelength anomalous diffraction based on the anomalous, signal of a cobalt ion measured on a conventional monochromatic X-ray, source. The unique absorption edge of cobalt (1.61 A) is compatible with, the Cu K alpha wavelength (1.54 A) commonly available in macromolecular, crystallography laboratories. This approach was applied to the, determination of the structure of Melampsora lini avirulence protein, AvrL567-A, a protein with a novel fold from the fungal pathogen flax rust, that induces plant disease resistance in flax plants. This approach using, cobalt ions may be applicable to all cobalt-binding proteins and may be, advantageous when synchrotron radiation is not readily available.
About this Structure
2OPC is a Single protein structure of sequence from Melampsora lini with and as ligands. Full crystallographic information is available from OCA.
Reference
The use of Co2+ for crystallization and structure determination, using a conventional monochromatic X-ray source, of flax rust avirulence protein., Guncar G, Wang CI, Forwood JK, Teh T, Catanzariti AM, Ellis JG, Dodds PN, Kobe B, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2007 Mar 1;63(Pt, 3):209-13. Epub 2007 Feb 23. PMID:17329816
Page seeded by OCA on Wed Jan 23 15:32:43 2008
