2qvt
From Proteopedia
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qvt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qvt OCA], [http://www.ebi.ac.uk/pdbsum/2qvt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qvt RCSB]</span> | ||
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[[Category: unknown function]] | [[Category: unknown function]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:53:51 2008'' |
Revision as of 01:53, 31 March 2008
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| , resolution 2.26Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of Melampsora lini avirulence protein, AvrL567-D
Overview
The gene-for-gene mechanism of plant disease resistance involves direct or indirect recognition of pathogen avirulence (Avr) proteins by plant resistance (R) proteins. Flax rust (Melampsora lini) AvrL567 avirulence proteins and the corresponding flax (Linum usitatissimum) L5, L6, and L7 resistance proteins interact directly. We determined the three-dimensional structures of two members of the AvrL567 family, AvrL567-A and AvrL567-D, at 1.4- and 2.3-A resolution, respectively. The structures of both proteins are very similar and reveal a beta-sandwich fold with no close known structural homologs. The polymorphic residues in the AvrL567 family map to the surface of the protein, and polymorphisms in residues associated with recognition differences for the R proteins lead to significant changes in surface chemical properties. Analysis of single amino acid substitutions in AvrL567 proteins confirm the role of individual residues in conferring differences in recognition and suggest that the specificity results from the cumulative effects of multiple amino acid contacts. The structures also provide insights into possible pathogen-associated functions of AvrL567 proteins, with nucleic acid binding activity demonstrated in vitro. Our studies provide some of the first structural information on avirulence proteins that bind directly to the corresponding resistance proteins, allowing an examination of the molecular basis of the interaction with the resistance proteins as a step toward designing new resistance specificities.
About this Structure
2QVT is a Single protein structure of sequence from Melampsora lini. Full crystallographic information is available from OCA.
Reference
Crystal structures of flax rust avirulence proteins AvrL567-A and -D reveal details of the structural basis for flax disease resistance specificity., Wang CI, Guncar G, Forwood JK, Teh T, Catanzariti AM, Lawrence GJ, Loughlin FE, Mackay JP, Schirra HJ, Anderson PA, Ellis JG, Dodds PN, Kobe B, Plant Cell. 2007 Sep;19(9):2898-912. Epub 2007 Sep 14. PMID:17873095
Page seeded by OCA on Mon Mar 31 04:53:51 2008
Categories: Melampsora lini | Single protein | Anderson, P A. | Catanzariti, A M. | Dodds, P N. | Ellis, J G. | Forwood, J K. | Guncar, G. | Kobe, B. | Lawrence, G. | Schirra, H J. | Teh, T. | Wang, C I. | Avrl567-a | Avrl567-d | Crystallization | Molecular replacement | Plant disease resistance | Unknown function
