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| | <StructureSection load='1s21' size='340' side='right'caption='[[1s21]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='1s21' size='340' side='right'caption='[[1s21]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1s21]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Psesh Psesh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S21 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1S21 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1s21]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_savastanoi_pv._phaseolicola Pseudomonas savastanoi pv. phaseolicola]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S21 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S21 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AvrPphF ORF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=319 PSESH])</td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1s21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s21 OCA], [https://pdbe.org/1s21 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s21 RCSB], [https://www.ebi.ac.uk/pdbsum/1s21 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s21 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1s21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s21 OCA], [http://pdbe.org/1s21 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s21 RCSB], [http://www.ebi.ac.uk/pdbsum/1s21 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s21 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [[https://www.uniprot.org/uniprot/Q9K2L5_PSESH Q9K2L5_PSESH]] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Psesh]] | + | [[Category: Pseudomonas savastanoi pv. phaseolicola]] |
| - | [[Category: Betts, L]] | + | [[Category: Betts L]] |
| - | [[Category: Chang, J H]] | + | [[Category: Chang JH]] |
| - | [[Category: Dangl, J K]] | + | [[Category: Dangl JK]] |
| - | [[Category: Desveaux, D]] | + | [[Category: Desveaux D]] |
| - | [[Category: Grant, S R]] | + | [[Category: Grant SR]] |
| - | [[Category: Nimchuk, Z]] | + | [[Category: Nimchuk Z]] |
| - | [[Category: Singer, A U]] | + | [[Category: Singer AU]] |
| - | [[Category: Sondek, J]] | + | [[Category: Sondek J]] |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Predominantly beta-strand]]
| + | |
| Structural highlights
Function
[Q9K2L5_PSESH]
Publication Abstract from PubMed
The avrPphF locus from Pseudomonas syringae pv. phaseolicola, the causative agent of bean halo-blight disease, encodes proteins which either enhance virulence on susceptible hosts or elicit defense responses on hosts carrying the R1 resistance gene. Here we present the crystal structures of the two proteins from the avrPphF operon. The structure of AvrPphF ORF1 is strikingly reminiscent of type III chaperones from bacterial pathogens of animals, indicating structural conservation of these specialized chaperones, despite high sequence divergence. The AvrPphF ORF2 effector adopts a novel "mushroom"-like structure containing "head" and "stalk" subdomains. The head subdomain possesses limited structural homology to the catalytic domain of bacterial ADP-ribosyltransferases (ADP-RTs), though no ADP-RT activity was detected for AvrPphF ORF2 in standard assays. Nonetheless, this structural similarity identified two clusters of conserved surface-exposed residues important for both virulence mediated by AvrPphF ORF2 and recognition of this effector by bean plants expressing the R1 resistance gene.
Crystal structures of the type III effector protein AvrPphF and its chaperone reveal residues required for plant pathogenesis.,Singer AU, Desveaux D, Betts L, Chang JH, Nimchuk Z, Grant SR, Dangl JL, Sondek J Structure. 2004 Sep;12(9):1669-81. PMID:15341731[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Singer AU, Desveaux D, Betts L, Chang JH, Nimchuk Z, Grant SR, Dangl JL, Sondek J. Crystal structures of the type III effector protein AvrPphF and its chaperone reveal residues required for plant pathogenesis. Structure. 2004 Sep;12(9):1669-81. PMID:15341731 doi:10.1016/j.str.2004.06.023
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