4eoy

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Current revision (11:04, 1 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4eoy]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EOY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EOY FirstGlance]. <br>
<table><tr><td colspan='2'>[[4eoy]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EOY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EOY 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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.22&#8491;</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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=4eoy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eoy OCA], [https://pdbe.org/4eoy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eoy RCSB], [https://www.ebi.ac.uk/pdbsum/4eoy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eoy 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=4eoy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eoy OCA], [https://pdbe.org/4eoy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eoy RCSB], [https://www.ebi.ac.uk/pdbsum/4eoy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eoy ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/Q8IJK2_PLAF7 Q8IJK2_PLAF7]]
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[https://www.uniprot.org/uniprot/Q8IJK2_PLAF7 Q8IJK2_PLAF7]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The autophagy-related proteins are thought to serve multiple functions in Plasmodium and are considered essential to parasite survival and development. We have studied two key interacting proteins, Atg8 and Atg3, of the autophagy pathway in Plasmodium falciparum. These proteins are vital for the formation and elongation of the autophagosome and essential to the process of macroautophagy. Autophagy may be required for conversion of the sporozoite into erythrocytic-infective merozoites and may be crucial for other functions during asexual blood stages. Here we describe the identification of an Atg8 family interacting motif (AIM) in Plasmodium Atg3, which binds Plasmodium Atg8. We determined the co-crystal structure of PfAtg8 with a short Atg3(1)(0)(3)(-)(1)(1)(0) peptide, corresponding to this motif, to 2.2 A resolution. Our in vitro interaction studies are in agreement with our X-ray crystal structure. Furthermore they suggest an important role for a unique Apicomplexan loop absent from human Atg8 homologues. Prevention of the protein-protein interaction of full length PfAtg8 with PfAtg3 was achieved at low micromolar concentrations with a small molecule, 1,2,3-trihydroxybenzene. Together our structural and interaction studies represent a starting point for future antimalarial drug discovery and design for this novel protein-protein interaction.
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Structural characterization and inhibition of the Plasmodium Atg8-Atg3 interaction.,Hain AU, Weltzer RR, Hammond H, Jayabalasingham B, Dinglasan RR, Graham DR, Colquhoun DR, Coppens I, Bosch J J Struct Biol. 2012 Dec;180(3):551-62. doi: 10.1016/j.jsb.2012.09.001. Epub 2012 , Sep 13. PMID:22982544<ref>PMID:22982544</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 4eoy" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Microtubule-associated protein 3D structures|Microtubule-associated protein 3D structures]]
*[[Microtubule-associated protein 3D structures|Microtubule-associated protein 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Plasmodium falciparum Atg8 in complex with Plasmodium falciparum Atg3 peptide

PDB ID 4eoy

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