4mit
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of E. histolytica RacC bound to the EhPAK4 PBD== | |
| + | <StructureSection load='4mit' size='340' side='right'caption='[[4mit]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4mit]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Entamoeba_histolytica_HM-1:IMSS-A Entamoeba histolytica HM-1:IMSS-A] and [https://en.wikipedia.org/wiki/Entamoeba_histolytica_HM-3:IMSS Entamoeba histolytica HM-3:IMSS]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MIT 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]] 2.35Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4mit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mit OCA], [https://pdbe.org/4mit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mit RCSB], [https://www.ebi.ac.uk/pdbsum/4mit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mit ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/RACC_ENTHI RACC_ENTHI] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Rho family GTPases modulate actin cytoskeleton dynamics by signaling through multiple effectors, including the p21-activated kinases (PAKs). The intestinal parasite Entamoeba histolytica expresses approximately 20 Rho family GTPases and seven isoforms of PAK, two of which have been implicated in pathogenesis-related processes such as amoebic motility and invasion and host cell phagocytosis. Here, we describe two previously unstudied PAK isoforms, EhPAK4 and EhPAK5, as highly specific effectors of EhRacC. A structural model based on 2.35 A X-ray crystallographic data of a complex between EhRacC(Q65L).GTP and the EhPAK4 p21 binding domain (PBD) reveals a fairly well-conserved Rho/effector interface despite deviation of the PBD alpha-helix. A structural comparison with EhRho1 in complex with EhFormin1 suggests likely determinants of Rho family GTPase signaling specificity in E. histolytica. These findings suggest a high degree of Rho family GTPase diversity and specificity in the single-cell parasite E. histolytica. Because PAKs regulate pathogenesis-related processes in E. histolytica, they may be valid pharmacologic targets for anti-amoebiasis drugs. | ||
| - | + | Entamoeba histolytica RacC Selectively Engages p21-Activated Kinase Effectors.,Bosch DE, Siderovski DP Biochemistry. 2015 Jan 20;54(2):404-12. doi: 10.1021/bi501226f. Epub 2015 Jan 2. PMID:25529118<ref>PMID:25529118</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4mit" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Entamoeba histolytica HM-1:IMSS-A]] | ||
| + | [[Category: Entamoeba histolytica HM-3:IMSS]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bosch DE]] | ||
| + | [[Category: Siderovski DP]] | ||
Current revision
Crystal structure of E. histolytica RacC bound to the EhPAK4 PBD
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