6w17

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Current revision (09:48, 2 April 2025) (edit) (undo)
 
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==Structure of Dip1-activated Arp2/3 complex with nucleated actin filament==
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<StructureSection load='6w17' size='340' side='right'caption='[[6w17]]' scene=''>
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<StructureSection load='6w17' size='340' side='right'caption='[[6w17]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6w17]] is a 17 chain structure with sequence from [https://en.wikipedia.org/wiki/Amanita_phalloides Amanita phalloides], [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] and [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6W17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6W17 FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6w17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6w17 OCA], [http://pdbe.org/6w17 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6w17 RCSB], [http://www.ebi.ac.uk/pdbsum/6w17 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6w17 ProSAT]</span></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">Electron Microscopy, [[Resolution|Resolution]] 3.9&#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=ALO:ALLO-THREONINE'>ALO</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=G5G:(2~{S},4~{S})-2-azanyl-4-methyl-4,5-bis(oxidanyl)pentanoic+acid'>G5G</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6w17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6w17 OCA], [https://pdbe.org/6w17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6w17 RCSB], [https://www.ebi.ac.uk/pdbsum/6w17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6w17 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ARP3_SCHPO ARP3_SCHPO] Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament (By similarity). May be involved in cytokinesis.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Arp2/3 complex, a crucial actin filament nucleator, undergoes structural rearrangements during activation by nucleation-promoting factors (NPFs). However, the conformational pathway leading to the nucleation-competent state is unclear due to lack of high-resolution structures of the activated state. Here we report a ~3.9 A resolution cryo-EM structure of activated Schizosaccharomyces pombe Arp2/3 complex bound to the S. pombe NPF Dip1 and attached to the end of the nucleated actin filament. The structure reveals global and local conformational changes that allow the two actin-related proteins in Arp2/3 complex to mimic a filamentous actin dimer and template nucleation. Activation occurs through a clamp-twisting mechanism, in which Dip1 forces two core subunits in Arp2/3 complex to pivot around one another, shifting half of the complex into a new activated position. By showing how Dip1 stimulates activation, the structure reveals how NPFs can activate Arp2/3 complex in diverse cellular processes.
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Cryo-EM reveals the transition of Arp2/3 complex from inactive to nucleation-competent state.,Shaaban M, Chowdhury S, Nolen BJ Nat Struct Mol Biol. 2020 Aug 24. pii: 10.1038/s41594-020-0481-x. doi:, 10.1038/s41594-020-0481-x. PMID:32839613<ref>PMID:32839613</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 6w17" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Actin-related protein 3D structures|Actin-related protein 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Amanita phalloides]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Z-disk]]
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[[Category: Oryctolagus cuniculus]]
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[[Category: Schizosaccharomyces pombe 972h-]]
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[[Category: Chowdhury S]]
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[[Category: Nolen BJ]]
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[[Category: Shaaban M]]

Current revision

Structure of Dip1-activated Arp2/3 complex with nucleated actin filament

PDB ID 6w17

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