Structural highlights
Publication Abstract from PubMed
The AvrRpt2 protein of the phytopathogenic bacterium Erwinia amylovora (AvrRpt2EA) is a secreted type III effector protein, which is recognised by the FB_MR5 resistance protein of Malusxrobusta 5, the only identified resistance protein from a Malus species preventing E. amylovora infection. The crystal structure of the immature catalytic domain of AvrRpt2EA, a C70 family cysteine protease and type III effector, was determined to a resolution of 1.85A. The structure provides insights into the cyclophilin-dependent activation of AvrRpt2, and identifies a cryptic leucine of a non-canonical cyclophilin binding motif. The structure also suggests that residue Cys156, responsible for the gene induced resistance, is not involved in substrate determination, and hints that recognition by FB_MR5 is due to direct interaction.
The structure of Erwinia amylovora AvrRpt2 provides insight into protein maturation and induced resistance to fire blight by Malusxrobusta 5.,Bartho JD, Demitri N, Bellini D, Flachowsky H, Peil A, Walsh MA, Benini S J Struct Biol. 2019 Mar 27. pii: S1047-8477(19)30064-4. doi:, 10.1016/j.jsb.2019.03.010. PMID:30928616[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bartho JD, Demitri N, Bellini D, Flachowsky H, Peil A, Walsh MA, Benini S. The structure of Erwinia amylovora AvrRpt2 provides insight into protein maturation and induced resistance to fire blight by Malusxrobusta 5. J Struct Biol. 2019 Mar 27. pii: S1047-8477(19)30064-4. doi:, 10.1016/j.jsb.2019.03.010. PMID:30928616 doi:http://dx.doi.org/10.1016/j.jsb.2019.03.010
