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The structure of Erwinia amylovora AvrRpt2 provides insight into protein maturation and induced resistance to fire blight by Malus × robusta 5
DOI:
10.1016/j.jsb.2019.03.010
Authors:
Joseph D.
Bartho
(Free University of Bolzano)
,
Nicola
Demitri
(Elettra – Sincrotrone Trieste)
,
Dom
Bellini
(Diamond Light Source; Research Complex at Harwell)
,
Henryk
Flachowsky
(Julius Kühn-Institut)
,
Andreas
Peil
(Julius Kühn-Institut)
,
Martin
Walsh
(Diamond Light Source)
,
Stefano
Benini
(Free University of Bolzano)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Journal Of Structural Biology
State:
Published (Approved)
Published:
March 2019
Abstract: 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 Malus × robusta 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 1.85 Å. 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.
Journal Keywords: Cysteine protease; Effector; T3SS; Cyclophilin; Plant resistance
Subject Areas:
Biology and Bio-materials
Facility: Elettra Sincrotrone
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Technical Tags: