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< | ==Structure of the Pto-binding domain of HopPmaL generated by limited thermolysin digestion== | ||
<StructureSection load='3svi' size='340' side='right'caption='[[3svi]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3svi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_syringae_pv._maculicola_str._ES4326 Pseudomonas syringae pv. maculicola str. ES4326]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SVI FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3svi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3svi OCA], [https://pdbe.org/3svi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3svi RCSB], [https://www.ebi.ac.uk/pdbsum/3svi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3svi ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
HopPmaL is a member of the HopAB family of type III effectors present in the phytopathogen Pseudomonas syringae. Using both X-ray crystallography and solution nuclear magnetic resonance, we demonstrate that HopPmaL contains two structurally homologous yet functionally distinct domains. The N-terminal domain corresponds to the previously described Pto-binding domain, while the previously uncharacterised C-terminal domain spans residues 308-385. While structurally similar, these domains do not share significant sequence similarity and most importantly demonstrate significant differences in key residues involved in host protein recognition, suggesting that each of them targets a different host protein. | |||
Structural Analysis of HopPmaL Reveals the Presence of a Second Adaptor Domain Common to the HopAB Family of Pseudomonas syringae Type III Effectors.,Singer AU, Wu B, Yee A, Houliston S, Xu X, Cui H, Skarina T, Garcia M, Semesi A, Arrowsmith CH, Savchenko A Biochemistry. 2012 Jan 10;51(1):1-3. Epub 2011 Dec 28. PMID:22191472<ref>PMID:22191472</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
== | </div> | ||
[[ | <div class="pdbe-citations 3svi" style="background-color:#fffaf0;"></div> | ||
[[Category: Pseudomonas syringae]] | == References == | ||
[[Category: Cui | <references/> | ||
[[Category: Edwards | __TOC__ | ||
[[Category: Joachimiak | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Savchenko | [[Category: Pseudomonas syringae pv. maculicola str. ES4326]] | ||
[[Category: Singer | [[Category: Cui H]] | ||
[[Category: Stein | [[Category: Edwards AM]] | ||
[[Category: Xu | [[Category: Joachimiak A]] | ||
[[Category: Savchenko A]] | |||
[[Category: Singer AU]] | |||
[[Category: Stein A]] | |||
[[Category: Xu X]] | |||
Latest revision as of 05:25, 21 November 2024
Structure of the Pto-binding domain of HopPmaL generated by limited thermolysin digestionStructure of the Pto-binding domain of HopPmaL generated by limited thermolysin digestion
Structural highlights
Publication Abstract from PubMedHopPmaL is a member of the HopAB family of type III effectors present in the phytopathogen Pseudomonas syringae. Using both X-ray crystallography and solution nuclear magnetic resonance, we demonstrate that HopPmaL contains two structurally homologous yet functionally distinct domains. The N-terminal domain corresponds to the previously described Pto-binding domain, while the previously uncharacterised C-terminal domain spans residues 308-385. While structurally similar, these domains do not share significant sequence similarity and most importantly demonstrate significant differences in key residues involved in host protein recognition, suggesting that each of them targets a different host protein. Structural Analysis of HopPmaL Reveals the Presence of a Second Adaptor Domain Common to the HopAB Family of Pseudomonas syringae Type III Effectors.,Singer AU, Wu B, Yee A, Houliston S, Xu X, Cui H, Skarina T, Garcia M, Semesi A, Arrowsmith CH, Savchenko A Biochemistry. 2012 Jan 10;51(1):1-3. Epub 2011 Dec 28. PMID:22191472[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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