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.

5l7s

From Proteopedia

Jump to: navigation, search

Crystal structure of RXLR effector PexRD54 from Phytophthora infestans

Structural highlights

5l7s is a 1 chain structure with sequence from Phytophthora infestans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.9Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RD54_PHYIT Effector that specifically binds host autophagy protein ATG8CL of the ATG8 family to stimulate autophagosome formation and subsequent autophagy rather than blocking autophagic flux (PubMed:26765567, PubMed:29932422). The pathogen remodels host-microbe interface by co-opting the host autophagy machinery which plays a key role in plant immunity (PubMed:29932422). PexRD54 competes with the autophagy cargo receptor Joka2 to deplete it out of ATG8CL complexes and interferes with Joka2's positive effect on pathogen defense (PubMed:26765567, PubMed:29932422).^[1] ^[2]

Publication Abstract from PubMed

Filamentous plant pathogens deliver effector proteins to host cells to promote infection. The Phytophthora infestans RXLR-type effector PexRD54 binds potato ATG8 via its ATG8-family interacting motif (AIM) and perturbs host selective autophagy. However, the structural basis of this interaction remains unknown. Here we define the crystal structure of PexRD54, which comprises a modular architecture including five tandem repeat domains, with the AIM sequence presented at the disordered C-terminus. To determine the interface between PexRD54 and ATG8, we solved the crystal structure of potato ATG8CL in complex with a peptide comprising the effectors AIM sequence, and established a model of the full-length PexRD54/ATG8CL complex using small angle X-ray scattering. Structure-informed deletion of the PexRD54 tandem domains reveals retention of ATG8CL binding in vitro and in planta. This study offers new insights into structure/function relationships of oomycete RXLR effectors and how these proteins engage with host cell targets to promote disease.

Structural basis of host Autophagy-related protein 8 (ATG8) binding by the Irish potato famine pathogen effector protein PexRD54.,Maqbool A, Hughes RK, Dagdas YF, Tregidgo N, Zess E, Belhaj K, Round A, Bozkurt TO, Kamoun S, Banfield MJ J Biol Chem. 2016 Jul 25. pii: jbc.M116.744995. PMID:27458016^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Dagdas YF, Belhaj K, Maqbool A, Chaparro-Garcia A, Pandey P, Petre B, Tabassum N, Cruz-Mireles N, Hughes RK, Sklenar J, Win J, Menke F, Findlay K, Banfield MJ, Kamoun S, Bozkurt TO. An effector of the Irish potato famine pathogen antagonizes a host autophagy cargo receptor. Elife. 2016 Jan 14;5:e10856. PMID:26765567 doi:10.7554/eLife.10856
↑ Dagdas YF, Pandey P, Tumtas Y, Sanguankiattichai N, Belhaj K, Duggan C, Leary AY, Segretin ME, Contreras MP, Savage Z, Khandare VS, Kamoun S, Bozkurt TO. Host autophagy machinery is diverted to the pathogen interface to mediate focal defense responses against the Irish potato famine pathogen. Elife. 2018 Jun 22;7:e37476. PMID:29932422 doi:10.7554/eLife.37476
↑ Maqbool A, Hughes RK, Dagdas YF, Tregidgo N, Zess E, Belhaj K, Round A, Bozkurt TO, Kamoun S, Banfield MJ. Structural basis of host Autophagy-related protein 8 (ATG8) binding by the Irish potato famine pathogen effector protein PexRD54. J Biol Chem. 2016 Jul 25. pii: jbc.M116.744995. PMID:27458016 doi:http://dx.doi.org/10.1074/jbc.M116.744995