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==Crystal structure of E. histolytica RacC bound to the EhPAK4 PBD==
==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 ==
== 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 [http://en.wikipedia.org/wiki/Entamoeba_histolytica_hm-1:imss-a Entamoeba histolytica hm-1:imss-a] and [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MIT FirstGlance]. <br>
</td></tr><tr id='ligand'><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></td></tr>
</td></tr><tr id='ligand'><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></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EhRacC, KM1_331620 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=885315 Entamoeba histolytica HM-3:IMSS]), EHI7A_018700, EhPAK4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=885318 Entamoeba histolytica HM-1:IMSS-A])</td></tr>
<tr id='activity'><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='activity'><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='resources'><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://pdbe.org/4mit PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mit RCSB], [http://www.ebi.ac.uk/pdbsum/4mit PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mit ProSAT]</span></td></tr>
<tr id='resources'><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://pdbe.org/4mit PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mit RCSB], [http://www.ebi.ac.uk/pdbsum/4mit PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mit ProSAT]</span></td></tr>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Entamoeba histolytica hm-1:imss-a]]
[[Category: Entamoeba histolytica hm-3:imss]]
[[Category: Large Structures]]
[[Category: Small monomeric GTPase]]
[[Category: Small monomeric GTPase]]
[[Category: Bosch, D E]]
[[Category: Bosch, D E]]

Revision as of 11:08, 10 April 2019

Crystal structure of E. histolytica RacC bound to the EhPAK4 PBDCrystal structure of E. histolytica RacC bound to the EhPAK4 PBD

Structural highlights

4mit is a 8 chain structure with sequence from Entamoeba histolytica hm-1:imss-a and Entamoeba histolytica hm-3:imss. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:EhRacC, KM1_331620 (Entamoeba histolytica HM-3:IMSS), EHI7A_018700, EhPAK4 (Entamoeba histolytica HM-1:IMSS-A)
Activity:Small monomeric GTPase, with EC number 3.6.5.2
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Bosch DE, Siderovski DP. Entamoeba histolytica RacC Selectively Engages p21-Activated Kinase Effectors. Biochemistry. 2015 Jan 20;54(2):404-12. doi: 10.1021/bi501226f. Epub 2015 Jan 2. PMID:25529118 doi:http://dx.doi.org/10.1021/bi501226f

4mit, resolution 2.35Å

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