2OPC

Structure of Melampsora lini avirulence protein, AvrL567-A

Summary for 2OPC

• Entry DOI: 10.2210/pdb2opc/pdb
• Descriptor: AvrL567-A, COBALT (II) ION, IMIDAZOLE, ... (4 entities in total)
• Functional Keywords: avrl567-a, cobalt, crystallization, single-wavelength anomalous dispersion (sad), plant disease resistance, protein binding, metal binding protein
• Biological source: Melampsora lini (flax rust)
• Total number of polymer chains: 1
• Total formula weight: 14658.52

Authors

Guncar, G.,Wang, C.I.,Forwood, J.K.,Teh, T.,Catanzariti, A.M.,Ellis, J.G.,Dodds, P.N.,Kobe, B. (deposition date: 2007-01-29, release date: 2007-03-06, Last modification date: 2023-12-27)

Primary citation

Guncar, G.,Wang, C.I.,Forwood, J.K.,Teh, T.,Catanzariti, A.M.,Ellis, J.G.,Dodds, P.N.,Kobe, B.
The use of Co2+ for crystallization and structure determination, using a conventional monochromatic X-ray source, of flax rust avirulence protein.
Acta Crystallogr.,Sect.F, 63:209-213, 2007

PubMed Abstract: 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.

PubMed: 17329816
DOI: 10.1107/S1744309107004599

Experimental method

X-RAY DIFFRACTION (1.43 Å)