4mit: Difference between revisions

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 ==Crystal structure of E. histolytica RacC bound to the EhPAK4 PBD==
-<StructureSection load='4mit' size='340' side='right' caption='[[4mit]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
+<StructureSection load='4mit' size='340' side='right'caption='[[4mit]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4mit]] is a 8 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MIT FirstGlance]. <br>
+<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><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><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]] 2.35&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Small_monomeric_GTPase Small monomeric GTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.2 3.6.5.2] </span></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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mit OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mit RCSB], [http://www.ebi.ac.uk/pdbsum/4mit PDBsum]</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=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>
+</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&reg;/PubMed&reg;, 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: Small monomeric GTPase]]
+[[Category: Entamoeba histolytica HM-1:IMSS-A]]
-[[Category: Bosch, D E.]]
+[[Category: Entamoeba histolytica HM-3:IMSS]]
-[[Category: Siderovski, D P.]]
+[[Category: Large Structures]]
-[[Category: Crib motif]]
+[[Category: Bosch DE]]
-[[Category: G domain]]
+[[Category: Siderovski DP]]
-[[Category: Gtp binding]]
-[[Category: Hydrolase]]
-[[Category: Kinase]]
-[[Category: P21 binding domain]]
-[[Category: Signaling protein]]