We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.
From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2qvt.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2qvt.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2qvt| PDB=2qvt | SCENE= }} | | {{STRUCTURE_2qvt| PDB=2qvt | SCENE= }} |
| | | | |
| - | '''Structure of Melampsora lini avirulence protein, AvrL567-D'''
| + | ===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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_17873095}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17873095 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_17873095}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 39: |
Line 43: |
| | [[Category: Plant disease resistance]] | | [[Category: Plant disease resistance]] |
| | [[Category: Unknown function]] | | [[Category: Unknown function]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 15:46:32 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:06:49 2008'' |
Revision as of 06:06, 28 July 2008
Template:STRUCTURE 2qvt
Structure of Melampsora lini avirulence protein, AvrL567-D
Template:ABSTRACT PUBMED 17873095
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 Jul 28 09:06:49 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