3q2b: Difference between revisions

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-[[Image:3q2b.jpg|left|200px]]
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+==Crystal Structure of an Actin Depolymerizing Factor==
-The line below this paragraph, containing "STRUCTURE_3q2b", creates the "Structure Box" on the page.
+<StructureSection load='3q2b' size='340' side='right'caption='[[3q2b]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3q2b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_HB3 Plasmodium falciparum HB3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q2B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q2B FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#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=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene></td></tr>
-{{STRUCTURE_3q2b|  PDB=3q2b  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3q2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q2b OCA], [https://pdbe.org/3q2b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q2b RCSB], [https://www.ebi.ac.uk/pdbsum/3q2b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q2b ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CADF1_PLAFX CADF1_PLAFX] Not involved in actin polymerisation, instead functions to stimulate nucleotide exchange on monomeric actin and influence turnover of the small amount of cytosolic actin microfilaments. Essential for erythrocytic schizogony.<ref>PMID:15975905</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Malaria parasite cell motility is a process that is dependent on the dynamic turnover of parasite-derived actin filaments. Despite its central role, actin's polymerization state is controlled by a set of identifiable regulators that is markedly reduced compared with those of other eukaryotic cells. In Plasmodium falciparum, the most virulent species that affects humans, this minimal repertoire includes two members of the actin-depolymerizing factor/cofilin (AC) family of proteins, P. falciparum actin-depolymerizing factor 1 (PfADF1) and P. falciparum actin-depolymerizing factor 2. This essential class of actin regulator is involved in the control of filament dynamics at multiple levels, from monomer binding through to filament depolymerization and severing. Previous biochemical analyses have suggested that PfADF1 sequesters monomeric actin but, unlike most eukaryotic counterparts, has limited potential to bind or depolymerize filaments. The molecular basis for these unusual properties and implications for parasite cell motility have not been established. Here we present the crystal structure of an apicomplexan AC protein, PfADF1. We show that PfADF1 lacks critical residues previously implicated as essential for AC-mediated actin filament binding and disassembly, having a substantially reduced filament-binding loop and C-terminal alpha4 helix. Despite this divergence in structure, we demonstrate that PfADF1 is capable of efficient actin filament severing. Furthermore, this severing occurs despite PfADF1's low binding affinity for filaments. Comparative structural analysis along with biochemical and microscopy evidence establishes that severing is reliant on the availability of an exposed basic residue in the filament-binding loop, a conserved minimal requirement that defines AC-mediated filament disassembly across eukaryotic cells.
-===Crystal Structure of an Actin Depolymerizing Factor===
+Minimal requirements for actin filament disassembly revealed by structural analysis of malaria parasite actin-depolymerizing factor 1.,Wong W, Skau CT, Marapana DS, Hanssen E, Taylor NL, Riglar DT, Zuccala ES, Angrisano F, Lewis H, Catimel B, Clarke OB, Kershaw NJ, Perugini MA, Kovar DR, Gulbis JM, Baum J Proc Natl Acad Sci U S A. 2011 Jun 14;108(24):9869-74. Epub 2011 May 31. PMID:21628589<ref>PMID:21628589</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_21628589}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 3q2b" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 21628589 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_21628589}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-[[3q2b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q2B OCA].
+[[Category: Plasmodium falciparum HB3]]
+[[Category: Baum J]]
-==Reference==
+[[Category: Clarke OB]]
-<ref group="xtra">PMID:021628589</ref><references group="xtra"/>
+[[Category: Gulbis JM]]
-[[Category: Plasmodium falciparum]]
+[[Category: Wong W]]
-[[Category: Baum, J.]]
-[[Category: Clarke, O B.]]
-[[Category: Gulbis, J M.]]
-[[Category: Wong, W.]]
-[[Category: Actin]]
-[[Category: Actin regulator]]
-[[Category: Actin-binding protein]]