Avirulence protein

From Proteopedia

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spinqualitylabelsall models Avirulence protein complex with ADP (stick model) and Tris (PDB code 2nun). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Avirulence protein (Avr) are produced by plant pathogens which subvert host cell biology upon infection. Avrs are small proteins which are recognized by the host cell resistance proteins. Avrs are effectors involved in pathogenicity. They are triggering the plant immune system. Avr genes are subject to high-speed diversifying selection allowing the pathogen to diversify its effector repertoire and thus escape recognition by the cell resistance mechanism.[1] For more details see Type III effector AvrB complexed with ADP Type III effector AvrB complexed with a high-affinity RIN4 peptide Structural highlights in Avirulence protein (PDB code 2nun).[2] Water molecules are shown as red spheres. 3D structures of avirulence protein Avirulence protein 3D structures

3D structures of avirulence protein

Updated on 31-March-2019

1ukf – PsAvrPphB – Psudomonas syringae
3tjy – PsAvr Hopab3 (mutant)
2lf3 – PsAvr Hopab3 – NMR
4b6x – PsAvr RPS4
1nh1 – PsAvrB III
2nud - PsAvrB III + RIN4 polypeptide
2nun - PsAvrB III + ADP
4fpr – Avr LM4-7 (mutant) – blackleg fungus
2ypf – AvrB III + DNA – Xanthomonas campestris
1r5e – PsAvrPto – NMR
2qkw – PsAvrPto + protein kinase
2fd4 – PsAvrPtoB C terminal
3hgl – PsAvrPtoB residues 121-205
3hgk - PsAvrPtoB + protein kinase
3tl8 - PsAvrPtoB + BAK1
2kq5 – AvrPthA residues 629-679 – Xanthomonas axonopodis – NMR
3rmr – HpAvrAtr1 – Hyaloperonospora parasitica
2lai - HpAvrAtr13 residues 54-154 - NMR
5vjj – Avr residues 23-111 – rust fungus

References

1. ↑ Zhu M, Shao F, Innes RW, Dixon JE, Xu Z. The crystal structure of Pseudomonas avirulence protein AvrPphB: a papain-like fold with a distinct substrate-binding site. Proc Natl Acad Sci U S A. 2004 Jan 6;101(1):302-7. Epub 2003 Dec 23. PMID:14694194 doi:10.1073/pnas.2036536100
2. ↑ Desveaux D, Singer AU, Wu AJ, McNulty BC, Musselwhite L, Nimchuk Z, Sondek J, Dangl JL. Type III effector activation via nucleotide binding, phosphorylation, and host target interaction. PLoS Pathog. 2007 Mar;3(3):e48. PMID:17397263 doi:10.1371/journal.ppat.0030048