2nar: Difference between revisions
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<StructureSection load='2nar' size='340' side='right' caption='[[2nar]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | <StructureSection load='2nar' size='340' side='right' caption='[[2nar]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2nar]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NAR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NAR FirstGlance]. <br> | <table><tr><td colspan='2'>[[2nar]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Botrytis_infestans Botrytis infestans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NAR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NAR FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nar FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nar OCA], [http://pdbe.org/2nar PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nar RCSB], [http://www.ebi.ac.uk/pdbsum/2nar PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2nar ProSAT]</span></td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Avr3a, PI35.0050, PI49.0530, putative ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4787 Botrytis infestans])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nar FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nar OCA], [http://pdbe.org/2nar PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nar RCSB], [http://www.ebi.ac.uk/pdbsum/2nar PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2nar ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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 Phytophthora infestans 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 Plasmodium falciparum 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. | |||
The RxLR Motif of the Host Targeting Effector AVR3a of Phytophthora infestans Is Cleaved before Secretion.,Wawra S, Trusch F, Matena A, Apostolakis K, Linne U, Zhukov I, Stanek J, Kozminski W, Davidson I, Secombes CJ, Bayer P, van West P Plant Cell. 2017 Jun;29(6):1184-1195. doi: 10.1105/tpc.16.00552. Epub 2017 May, 18. PMID:28522546<ref>PMID:28522546</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2nar" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Botrytis infestans]] | |||
[[Category: Bayer, P]] | [[Category: Bayer, P]] | ||
[[Category: Kozminski, W]] | [[Category: Kozminski, W]] | ||
Revision as of 09:05, 6 June 2018
Solution structure of AVR3a_60-147 from Phytophthora infestansSolution structure of AVR3a_60-147 from Phytophthora infestans
Structural highlights
Publication Abstract from PubMedWhen 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 Phytophthora infestans 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 Plasmodium falciparum 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. The RxLR Motif of the Host Targeting Effector AVR3a of Phytophthora infestans Is Cleaved before Secretion.,Wawra S, Trusch F, Matena A, Apostolakis K, Linne U, Zhukov I, Stanek J, Kozminski W, Davidson I, Secombes CJ, Bayer P, van West P Plant Cell. 2017 Jun;29(6):1184-1195. doi: 10.1105/tpc.16.00552. Epub 2017 May, 18. PMID:28522546[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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