1r5e: Difference between revisions
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==Solution structure of the folded core of Pseudomonas syringae effector protein, AvrPto== | |||
<StructureSection load='1r5e' size='340' side='right'caption='[[1r5e]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1r5e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_syringae Pseudomonas syringae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R5E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R5E FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1r5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r5e OCA], [https://pdbe.org/1r5e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r5e RCSB], [https://www.ebi.ac.uk/pdbsum/1r5e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r5e ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q08242_PSESX Q08242_PSESX] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Pseudomonas syringae pv. tomato, the causative agent of bacterial speck disease of tomato, uses a type III secretion system (TTSS) to deliver effector proteins into the host cell. In resistant plants, the bacterial effector protein AvrPto physically interacts with the host Pto kinase and elicits antibacterial defense responses. In susceptible plants, which lack the Pto kinase, AvrPto acts as a virulence factor to promote bacterial growth. The solution structure of AvrPto reveals a functional core consisting of a three-helix bundle motif flanked by disordered N- and C-terminal tails. Residues required for Pto binding lie in a 19 residue Omega loop. Modeling suggests a hydrophobic patch involving the activation loop of Pto forms a contact surface with the AvrPto Omega loop and that helix packing mediates interactions between AvrPto and putative virulence targets Api2 and Api3. The AvrPto structure has a low stability that may facilitate chaperone-independent secretion by the TTSS. | |||
The solution structure of type III effector protein AvrPto reveals conformational and dynamic features important for plant pathogenesis.,Wulf J, Pascuzzi PE, Fahmy A, Martin GB, Nicholson LK Structure. 2004 Jul;12(7):1257-68. PMID:15242602<ref>PMID:15242602</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1r5e" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Avirulence protein 3D structures|Avirulence protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pseudomonas syringae]] | [[Category: Pseudomonas syringae]] | ||
[[Category: Martin GB]] | |||
[[Category: Martin | [[Category: Nicholson LK]] | ||
[[Category: Nicholson | [[Category: Pascuzzi PE]] | ||
[[Category: Pascuzzi | [[Category: Wulf J]] | ||
[[Category: Wulf | |||
Latest revision as of 12:03, 22 May 2024
Solution structure of the folded core of Pseudomonas syringae effector protein, AvrPtoSolution structure of the folded core of Pseudomonas syringae effector protein, AvrPto
Structural highlights
FunctionPublication Abstract from PubMedPseudomonas syringae pv. tomato, the causative agent of bacterial speck disease of tomato, uses a type III secretion system (TTSS) to deliver effector proteins into the host cell. In resistant plants, the bacterial effector protein AvrPto physically interacts with the host Pto kinase and elicits antibacterial defense responses. In susceptible plants, which lack the Pto kinase, AvrPto acts as a virulence factor to promote bacterial growth. The solution structure of AvrPto reveals a functional core consisting of a three-helix bundle motif flanked by disordered N- and C-terminal tails. Residues required for Pto binding lie in a 19 residue Omega loop. Modeling suggests a hydrophobic patch involving the activation loop of Pto forms a contact surface with the AvrPto Omega loop and that helix packing mediates interactions between AvrPto and putative virulence targets Api2 and Api3. The AvrPto structure has a low stability that may facilitate chaperone-independent secretion by the TTSS. The solution structure of type III effector protein AvrPto reveals conformational and dynamic features important for plant pathogenesis.,Wulf J, Pascuzzi PE, Fahmy A, Martin GB, Nicholson LK Structure. 2004 Jul;12(7):1257-68. PMID:15242602[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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