6a9c: Difference between revisions
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<StructureSection load='6a9c' size='340' side='right'caption='[[6a9c]], [[Resolution|resolution]] 1.98Å' scene=''> | <StructureSection load='6a9c' size='340' side='right'caption='[[6a9c]], [[Resolution|resolution]] 1.98Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6a9c]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A9C OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6a9c]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Entamoeba_histolytica Entamoeba histolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A9C FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=6a9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a9c OCA], [https://pdbe.org/6a9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a9c RCSB], [https://www.ebi.ac.uk/pdbsum/6a9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a9c ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/C4LUC7_ENTH1 C4LUC7_ENTH1] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6a9c" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6a9c" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Myosin 3D Structures|Myosin 3D Structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Entamoeba histolytica]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Gautam | [[Category: Gautam G]] | ||
[[Category: Gourinath | [[Category: Gourinath S]] | ||
Latest revision as of 12:21, 22 November 2023
Crystal Structure c-terminal SH3 domain of Myosin IB from Entamoeba histolytica bound to EhFP10(GEF) peptide.Crystal Structure c-terminal SH3 domain of Myosin IB from Entamoeba histolytica bound to EhFP10(GEF) peptide.
Structural highlights
FunctionPublication Abstract from PubMedMotility and phagocytosis are key processes that are involved in invasive amoebiasis disease caused by intestinal parasite Entamoeba histolytica. Previous studies have reported unconventional myosins to play significant role in membrane based motility as well as endocytic processes. EhMyosin IB is the only unconventional myosin present in E. histolytica, is thought to be involved in both of these processes. Here, we report an interaction between the SH3 domain of EhMyosin IB and c-terminal domain of EhFP10, a Rho guanine nucleotide exchange factor. EhFP10 was found to be confined to Entamoeba species only, and to contain a c-terminal domain that binds and bundles actin filaments. EhFP10 was observed to localize in the membrane ruffles, phagocytic and macropinocytic cups of E. histolytica trophozoites. It was also found in early pinosomes but not early phagosomes. A crystal structure of the c-terminal SH3 domain of EhMyosin IB (EhMySH3) in complex with an EhFP10 peptide and co-localization studies established the interaction of EhMySH3 with EhFP10. This interaction was shown to lead to inhibition of actin bundling activity and to thereby regulate actin dynamics during endocytosis. We hypothesize that unique domain architecture of EhFP10 might be compensating the absence of Wasp and related proteins in Entamoeba, which are known partners of myosin SH3 domains in other eukaryotes. Our findings also highlights the role of actin bundling during endocytosis. EhFP10: A FYVE family GEF interacts with myosin IB to regulate cytoskeletal dynamics during endocytosis in Entamoeba histolytica.,Gautam G, Ali MS, Bhattacharya A, Gourinath S PLoS Pathog. 2019 Feb 19;15(2):e1007573. doi: 10.1371/journal.ppat.1007573., eCollection 2019 Feb. PMID:30779788[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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