Structures of Phytophthora RXLR effector proteins: a conserved but adaptable fold underpins functional diversity

Boutemy, Laurence S., King, Stuart R. F., Win, Joe, Hughes, Richard K., Clarke, Thomas A. ORCID: https://orcid.org/0000-0002-6234-1914, Blumenschein, Tharin M. A. ORCID: https://orcid.org/0000-0002-4932-5178, Kamoun, Sophien ORCID: https://orcid.org/0000-0002-0290-0315 and Banfield, Mark J. (2011) Structures of Phytophthora RXLR effector proteins: a conserved but adaptable fold underpins functional diversity. Journal of Biological Chemistry, 286 (41). pp. 35834-35842. ISSN 0021-9258

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Abstract

Phytopathogens deliver effector proteins inside host plant cells to promote infection. These proteins can also be sensed by the plant immune system, leading to restriction of pathogen growth. Effector genes can display signatures of positive selection and rapid evolution, presumably a consequence of their co-evolutionary arms race with plants. The molecular mechanisms underlying how effectors evolve to gain new virulence functions and/or evade the plant immune system are poorly understood. Here, we report the crystal structures of the effector domains from two oomycete RXLR proteins, Phytophthora capsici AVR3a11 and Phytophthora infestans PexRD2. Despite sharing

Item Type: Article
Faculty \ School: Faculty of Science > The Sainsbury Laboratory
Faculty of Science > School of Biological Sciences
Faculty of Science > School of Chemistry
UEA Research Groups: Faculty of Science > Research Groups > Molecular Microbiology
Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017)
Faculty of Science > Research Groups > Plant Sciences
Faculty of Science > Research Groups > Chemistry of Life Processes
Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry
Faculty of Science > Research Groups > Energy Materials Laboratory
Depositing User: Users 2731 not found.
Date Deposited: 24 Jan 2012 15:17
Last Modified: 17 Jan 2024 01:19
URI: https://ueaeprints.uea.ac.uk/id/eprint/36454
DOI: 10.1074/jbc.M111.262303

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