References
Abramovitch RB, Janjusevic R, Stebbins CE, Martin GR (2006) Type III effector AvrPtoB requires intrinsic E3 ubiquitin ligase activity to suppress plant cell death and immunity. Proc Natl Acad Sci USA 103:2851–2856
Brunger AT, Adams PD, Clore GM, DeLano WL, Gros P, Grosse-Kunstleve RW, Jiang J-S, Kuszewski J, Nilges M, Pannu NS, Read RJ, Rice LM, Simonson T, Warren GL (1998) Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr Sect D 54:905–921
Chisholm ST, Coaker G, Day B, Staskawicz BJ (2006) Host–microbe interactions: shaping the evolution of the plant immune response. Cell 124:803–814
Cornilescu G, Delaglio F, Bax A (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR 13:289–302
Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293
Feng F, Yang F, Rong W, Wu X, Zhang J, Chen S, He C, Zhou J-M (2012) A Xanthomonas uridine 5′-monophosphate transferase inhibits plant immune kinases. Nature 485:114–120
Gunčar G, Wang C-IA, Forwood JK, The T, Catanzariti A-M, Lawrence GJ, Loughlin FE, Mackay JP, Schirra HJ, Anderson PA, Ellis JG, Dodds PN, Kobe B (2007) Adaptive evolution has targeted the C-terminal domain of the RXLR effectors of plant pathogenic oomycetes. Plant Cell 19:2898–2912
Holm L, Sander C (1993) Protein structure comparison by alignment of distance matrices. J Mol Biol 233:123–138
Jones JDG, Dangl JL (2006) The plant immune system. Nature 444:323–329
Laskowski RA, Rullmann JAC, MacArthur MW, Kaptein R, Thornton JM (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J Biomol NMR 8:477–486
Li W, Wang B, Wu J, Lu G, Hu Y, Zhang X, Zhang Z, Zhao Q, Feng Q, Zhang H, Wang Z, Wang G, Hna B, Wang Z, Zhou B (2009) The Magnaporthe oryzae avirulence gene AvrPiz-t encodes a predicted secreted protein that triggers the immunity in rice mediated by the blast resistance gene Piz-t. Mol Plant Microbe Interact 22:411–420
Li P, Dong B, Zhou H, Zhou B (2012) Functional analysis of cysteine residues of the Magnaporthe oryzae avirulence protein AvrPiz-t. Acta Phytopathologica Sinica 42:474–479
Park C-H, Chen S, Shirsekar G, Zhou B, Khang CH, Songkumarn P, Ning Y, Bellizzi M, Valent B, Wang G-L (2012) The Magnaporthe oryzae effector AvrPiz-t targets the RING E3 ubiquitin ligase APIP6 to suppress pathogen-associated molecular pattern-triggered immunity in rice. Plant Cell. doi:10.1105/tpc.112.105429
Rieping W, Habeck M, Bardiaux B, Bernard A, Malliavin TE, Nilges M (2007) ARIA2: automated NOE assignment and data integration in NMR structure. Bioinformatics 23:318–382
Sarma GN, Manning VA, Ciuffetti LM, Karplus PA (2005) Structure of Ptr ToxA: an RGD-containing host-selective toxin from Pyrenophora tritici-repentis. Plant Cell 17:3190–3202
Wilton M, Subramaniam R, Elmore J, Gelsensteiner C, Coaker G, Desveaux D (2010) The type III effector HopF2Pto targets Arabidopsis RIN4 protein to promote Pseudomonas syringae virulence. Proc Natl Acad Sci USA 107:2349–2354
Wishart DS, Sykes BD (1994) The 13C Chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 4:171–180
Zhou B, Qu S, Liu G, Dolan M, Sakai H, Lu G, Bellizzi M, Wang G-L (2006) The eight amino-acid differences within three leucine-rich repeats between Pi2 and Piz-t resistance proteins determine the resistance specificity to Magnaporthe grisea. Mol Plant Microbe Interact 19:1216–1228
Acknowledgments
This work was supported by grants from the National Program on Key Basic Research of China (2009CB918600, to J. Z. and M. L.), the National Grand Project for Medicine Innovation (2011ZX09506-001) and the Natural Science Foundation in China (30971878, to B. Z.). We are grateful to Prof. Chunyang Cao and Yan Zhang for valuable suggestions in NMR structure determination. We also thank Dr. Wenyu Wen for her help on H/D exchange experiments.
Author information
Authors and Affiliations
Corresponding authors
Additional information
Zhi-Min Zhang and Xu Zhang contributed equally to the present work.
Electronic supplementary material
Below is the link to the electronic supplementary material.
Rights and permissions
About this article
Cite this article
Zhang, ZM., Zhang, X., Zhou, ZR. et al. Solution structure of the Magnaporthe oryzae avirulence protein AvrPiz-t. J Biomol NMR 55, 219–223 (2013). https://doi.org/10.1007/s10858-012-9695-5
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s10858-012-9695-5