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2NAR

Solution structure of AVR3a_60-147 from Phytophthora infestans

Summary for 2NAR
Entry DOI10.2210/pdb2nar/pdb
NMR InformationBMRB: 25944
DescriptorEffector protein Avr3a (1 entity in total)
Functional Keywordsprotein binding
Biological sourcePhytophthora infestans (potato late blight fungus)
Total number of polymer chains1
Total formula weight11511.08
Authors
Matena, A.,Bayer, P.,Zhukov, I.,Stanek, J.,Kozminski, W.,van West, P.,Wawra, S. (deposition date: 2016-01-08, release date: 2017-01-11, Last modification date: 2024-05-01)
Primary citationWawra, S.,Trusch, F.,Matena, A.,Apostolakis, K.,Linne, U.,Zhukov, I.,Stanek, J.,Kozminski, W.,Davidson, I.,Secombes, C.J.,Bayer, P.,van West, P.
The RxLR Motif of the Host Targeting Effector AVR3a ofPhytophthora infestansIs Cleaved before Secretion.
Plant Cell, 29:1184-1195, 2017
Cited by
PubMed Abstract: When plant-pathogenic oomycetes infect their hosts, they employ a large arsenal of effector proteins to establish a successful infection. Some effector proteins are secreted and are destined to be translocated and function inside host cells. The largest group of translocated proteins from oomycetes is the RxLR effectors, defined by their conserved N-terminal Arg-Xaa-Leu-Arg (RxLR) motif. However, the precise role of this motif in the host cell translocation process is unclear. Here, detailed biochemical studies of the RxLR effector AVR3a from the potato pathogen are presented. Mass spectrometric analysis revealed that the RxLR sequence of native AVR3a is cleaved off prior to secretion by the pathogen and the N terminus of the mature effector was found likely to be acetylated. High-resolution NMR structure analysis of AVR3a indicates that the RxLR motif is well accessible to potential processing enzymes. Processing and modification of AVR3a is to some extent similar to events occurring with the export element (PEXEL) found in malaria effector proteins from These findings imply a role for the RxLR motif in the secretion of AVR3a by the pathogen, rather than a direct role in the host cell entry process itself.
PubMed: 28522546
DOI: 10.1105/tpc.16.00552
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

245663

数据于2025-12-03公开中

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