3ref

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<StructureSection load='3ref' size='340' side='right'caption='[[3ref]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='3ref' size='340' side='right'caption='[[3ref]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ref]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enthi Enthi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3REF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3REF FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ref]] is a 2 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=3REF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3REF FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3reg|3reg]], [[1ftn|1ftn]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EhRho1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5759 ENTHI])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ref FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ref OCA], [https://pdbe.org/3ref PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ref RCSB], [https://www.ebi.ac.uk/pdbsum/3ref PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ref ProSAT]</span></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=3ref FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ref OCA], [https://pdbe.org/3ref PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ref RCSB], [https://www.ebi.ac.uk/pdbsum/3ref PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ref ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/RHO1_ENTHI RHO1_ENTHI]
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The single-celled human parasite Entamoeba histolytica possesses a dynamic actin cytoskeleton vital for its intestinal and systemic pathogenicity. The E. histolytica genome encodes several Rho family GTPases known to regulate cytoskeletal dynamics. EhRho1, the first family member identified, was reported to be insensitive to the Rho GTPase-specific Clostridium botulinum C3 exoenzyme, raising the possibility that it may be a misclassified Ras family member. Here, we report the crystal structures of EhRho1 in both active and inactive states. EhRho1 is activated by a conserved switch mechanism, but diverges from mammalian Rho GTPases in lacking a signature Rho insert helix. EhRho1 engages a homolog of mDia, EhFormin1, suggesting a role in mediating serum-stimulated actin reorganization and microtubule formation during mitosis. EhRho1, but not a constitutively active mutant, interacts with a newly identified EhRhoGDI in a prenylation-dependent manner. Furthermore, constitutively active EhRho1 induces actin stress fiber formation in mammalian fibroblasts, thereby identifying it as a functional Rho family GTPase. EhRho1 exhibits a fast rate of nucleotide exchange relative to mammalian Rho GTPases due to a distinctive switch one isoleucine residue reminiscent of the constitutively active F28L mutation in human Cdc42, which for the latter protein, is sufficient for cellular transformation. Nonconserved, nucleotide-interacting residues within EhRho1, revealed by the crystal structure models, were observed to contribute a moderating influence on fast spontaneous nucleotide exchange. Collectively, these observations indicate that EhRho1 is a bona fide member of the Rho GTPase family, albeit with unique structural and functional aspects compared with mammalian Rho GTPases.
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Unique structural and nucleotide exchange features of the Rho1 GTPase of Entamoeba histolytica.,Bosch DE, Wittchen ES, Qiu C, Burridge K, Siderovski DP J Biol Chem. 2011 Nov 11;286(45):39236-46. Epub 2011 Sep 19. PMID:21930699<ref>PMID:21930699</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3ref" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Enthi]]
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[[Category: Entamoeba histolytica]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bosch, D E]]
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[[Category: Bosch DE]]
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[[Category: Qiu, C]]
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[[Category: Qiu C]]
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[[Category: Siderovski, D P]]
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[[Category: Siderovski DP]]
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[[Category: Cytoskeleton]]
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[[Category: Gtp-binding]]
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[[Category: Lipoprotein]]
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[[Category: Nucleotide-binding]]
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[[Category: Prenylation]]
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[[Category: Signaling protein]]
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Current revision

Crystal structure of EhRho1 bound to GDP and Magnesium

PDB ID 3ref

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