6ui4: Difference between revisions
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==Crystal structure of phenamacril-bound F. graminearum myosin I== | |||
<StructureSection load='6ui4' size='340' side='right'caption='[[6ui4]], [[Resolution|resolution]] 2.65Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ui4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_graminearum_PH-1 Fusarium graminearum PH-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UI4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UI4 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]] 2.65Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=Q8V:ethyl+(~{Z})-3-azanyl-2-cyano-3-phenyl-prop-2-enoate'>Q8V</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=6ui4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ui4 OCA], [https://pdbe.org/6ui4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ui4 RCSB], [https://www.ebi.ac.uk/pdbsum/6ui4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ui4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/I1RCT2_GIBZE I1RCT2_GIBZE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Fusarium is a genus of filamentous fungi that includes species that cause devastating diseases in major staple crops, such as wheat, maize, rice, and barley, resulting in severe yield losses and mycotoxin contamination of infected grains. Phenamacril is a novel fungicide that is considered environmentally benign due to its exceptional specificity; it inhibits the ATPase activity of the sole class I myosin of only a subset of Fusarium species including the major plant pathogens F. graminearum, F. asiaticum and F. fujikuroi. To understand the underlying mechanisms of inhibition, species specificity, and resistance mutations, we have determined the crystal structure of phenamacril-bound F. graminearum myosin I. Phenamacril binds in the actin-binding cleft in a new allosteric pocket that contains the central residue of the regulatory Switch 2 loop and that is collapsed in the structure of a myosin with closed actin-binding cleft, suggesting that pocket occupancy blocks cleft closure. We have further identified a single, transferable phenamacril-binding residue found exclusively in phenamacril-sensitive myosins to confer phenamacril selectivity. | |||
Structural basis of Fusarium myosin I inhibition by phenamacril.,Zhou Y, Zhou XE, Gong Y, Zhu Y, Cao X, Brunzelle JS, Xu HE, Zhou M, Melcher K, Zhang F PLoS Pathog. 2020 Mar 12;16(3):e1008323. doi: 10.1371/journal.ppat.1008323. PMID:32163521<ref>PMID:32163521</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6ui4" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Calmodulin 3D structures|Calmodulin 3D structures]] | ||
[[Category: | *[[Myosin 3D Structures|Myosin 3D Structures]] | ||
[[Category: | == References == | ||
[[Category: Zhou | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Fusarium graminearum PH-1]] | |||
[[Category: Large Structures]] | |||
[[Category: Gong Y]] | |||
[[Category: Melcher K]] | |||
[[Category: Xu HE]] | |||
[[Category: Zhang F]] | |||
[[Category: Zhou M]] | |||
[[Category: Zhou XE]] | |||
[[Category: Zhou Y]] | |||
[[Category: Zhu Y]] | |||
Latest revision as of 13:32, 23 October 2024
Crystal structure of phenamacril-bound F. graminearum myosin ICrystal structure of phenamacril-bound F. graminearum myosin I
Structural highlights
FunctionPublication Abstract from PubMedFusarium is a genus of filamentous fungi that includes species that cause devastating diseases in major staple crops, such as wheat, maize, rice, and barley, resulting in severe yield losses and mycotoxin contamination of infected grains. Phenamacril is a novel fungicide that is considered environmentally benign due to its exceptional specificity; it inhibits the ATPase activity of the sole class I myosin of only a subset of Fusarium species including the major plant pathogens F. graminearum, F. asiaticum and F. fujikuroi. To understand the underlying mechanisms of inhibition, species specificity, and resistance mutations, we have determined the crystal structure of phenamacril-bound F. graminearum myosin I. Phenamacril binds in the actin-binding cleft in a new allosteric pocket that contains the central residue of the regulatory Switch 2 loop and that is collapsed in the structure of a myosin with closed actin-binding cleft, suggesting that pocket occupancy blocks cleft closure. We have further identified a single, transferable phenamacril-binding residue found exclusively in phenamacril-sensitive myosins to confer phenamacril selectivity. Structural basis of Fusarium myosin I inhibition by phenamacril.,Zhou Y, Zhou XE, Gong Y, Zhu Y, Cao X, Brunzelle JS, Xu HE, Zhou M, Melcher K, Zhang F PLoS Pathog. 2020 Mar 12;16(3):e1008323. doi: 10.1371/journal.ppat.1008323. PMID:32163521[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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