4efh

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4efh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acanthamoeba_castellanii Acanthamoeba castellanii] and [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EFH FirstGlance]. <br>
<table><tr><td colspan='2'>[[4efh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acanthamoeba_castellanii Acanthamoeba castellanii] and [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EFH 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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 2.48&#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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=4efh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4efh OCA], [https://pdbe.org/4efh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4efh RCSB], [https://www.ebi.ac.uk/pdbsum/4efh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4efh 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=4efh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4efh OCA], [https://pdbe.org/4efh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4efh RCSB], [https://www.ebi.ac.uk/pdbsum/4efh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4efh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/ACT1_ACACA ACT1_ACACA]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
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[https://www.uniprot.org/uniprot/ACT1_ACACA ACT1_ACACA] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Spire is a WH2 domain-containing actin nucleator essential for establishing an actin mesh during oogenesis. In vitro, in addition to nucleating filaments, Spire can sever them and sequester actin monomers. Understanding how Spire is capable of these disparate functions and which are physiologically relevant is an important goal. To study severing, we examined the effect of Drosophila Spire on preformed filaments in bulk and single filament assays. We observed rapid depolymerization of actin filaments by Spire, which we conclude is largely due to its sequestration activity and enhanced by its weak severing activity. We also studied the solution and crystal structures of Spire-actin complexes. We find structural and functional differences between constructs containing four WH2-domains (Spir-ABCD) and two WH2-domains (Spir-CD) that may provide insight into mechanisms of nucleation and sequestration. Intriguingly, we observed lateral interactions between actin monomers associated with Spir-ABCD, suggesting that the structures built by these four tandem WH2 domains are more complex than originally imagined. Finally, we propose that Spire-actin mixtures contain both nuclei and sequestration structures.
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Multiple forms of Spire-actin complexes and their functional consequences.,Chen CK, Sawaya MR, Phillips ML, Reisler E, Quinlan ME J Biol Chem. 2012 Feb 8. PMID:22334675<ref>PMID:22334675</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 4efh" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Actin 3D structures|Actin 3D structures]]
*[[Actin 3D structures|Actin 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Acanthamoeba Actin complex with Spir domain D

PDB ID 4efh

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