2xfa: Difference between revisions
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<StructureSection load='2xfa' size='340' side='right'caption='[[2xfa]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='2xfa' size='340' side='right'caption='[[2xfa]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2xfa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2xfa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_berghei Plasmodium berghei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XFA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XFA FirstGlance]. <br> | ||
</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=2xfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xfa OCA], [https://pdbe.org/2xfa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xfa RCSB], [https://www.ebi.ac.uk/pdbsum/2xfa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xfa ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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=2xfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xfa OCA], [https://pdbe.org/2xfa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xfa RCSB], [https://www.ebi.ac.uk/pdbsum/2xfa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xfa ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q3YPH0_PLABE Q3YPH0_PLABE] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Plasmodium berghei]] | ||
[[Category: Chatterjee | [[Category: Chatterjee M]] | ||
[[Category: Huttu | [[Category: Huttu J]] | ||
[[Category: Kursula | [[Category: Kursula I]] | ||
[[Category: Sattler | [[Category: Sattler JM]] | ||
[[Category: Schueler | [[Category: Schueler H]] | ||
[[Category: Singh | [[Category: Singh BK]] | ||
Latest revision as of 13:38, 16 August 2023
Crystal structure of Plasmodium berghei actin depolymerization factor 2Crystal structure of Plasmodium berghei actin depolymerization factor 2
Structural highlights
FunctionPublication Abstract from PubMedApicomplexan parasites, such as the malaria-causing Plasmodium, utilize an actin-based motor for motility and host cell invasion. The actin filaments of these parasites are unusually short, and actin polymerization is under strict control of a small set of regulatory proteins, which are poorly conserved with their mammalian orthologs. Actin depolymerization factors (ADFs) are among the most important actin regulators, affecting the rates of filament turnover in a multifaceted manner. Plasmodium has two ADFs that display low sequence homology with each other and with the higher eukaryotic family members. Here, we show that ADF2, like canonical ADF proteins but unlike ADF1, binds to both globular and filamentous actin, severing filaments and inducing nucleotide exchange on the actin monomer. The crystal structure of Plasmodium ADF1 shows major differences from the ADF consensus, explaining the lack of F-actin binding. Plasmodium ADF2 structurally resembles the canonical members of the ADF/cofilin family. Crystal structures explain functional differences in the two actin depolymerization factors of the malaria parasite.,Singh BK, Sattler JM, Chatterjee M, Huttu J, Schuler H, Kursula I J Biol Chem. 2011 Aug 12;286(32):28256-64. PMID:21832095[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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