3onx

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<StructureSection load='3onx' size='340' side='right'caption='[[3onx]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='3onx' size='340' side='right'caption='[[3onx]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3onx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ONX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ONX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3onx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ONX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ONX FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2.904&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3okq|3okq]]</div></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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AIP3, BUD6, L8543.5, YLR319C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3onx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3onx OCA], [https://pdbe.org/3onx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3onx RCSB], [https://www.ebi.ac.uk/pdbsum/3onx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3onx 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=3onx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3onx OCA], [https://pdbe.org/3onx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3onx RCSB], [https://www.ebi.ac.uk/pdbsum/3onx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3onx ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/BUD6_YEAST BUD6_YEAST]] Not essential for mitotic growth but is necessary for normal morphogenesis. Involved in the organization and/or function of the actin cytoskeleton.
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[https://www.uniprot.org/uniprot/BUD6_YEAST BUD6_YEAST] Not essential for mitotic growth but is necessary for normal morphogenesis. Involved in the organization and/or function of the actin cytoskeleton.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Formin proteins and their associated factors cooperate to assemble unbranched actin filaments in diverse cellular structures. The Saccharomyces cerevisiae formin Bni1 and its associated nucleation-promoting factor (NPF) Bud6 generate actin cables and mediate polarized cell growth. Bud6 binds to both the tail of the formin and G-actin, thereby recruiting monomeric actin to the formin to create a nucleation seed. Here, we structurally and functionally dissect the nucleation-promoting C-terminal region of Bud6 into a Bni1-binding "core" domain and a G-actin binding "flank" domain. The approximately 2-A resolution crystal structure of the Bud6 core domain reveals an elongated dimeric rod with a unique fold resembling a triple-helical coiled-coil. Binding and actin-assembly assays show that conserved residues on the surface of this domain mediate binding to Bni1 and are required for NPF activity. We find that the Bni1 dimer binds two Bud6 dimers and that the Bud6 flank binds a single G-actin molecule. These findings suggest a model in which a Bni1/Bud6 complex with a 2:4 subunit stoichiometry assembles a nucleation seed with Bud6 coordinating up to four actin subunits.
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Structure of the formin-interaction domain of the actin nucleation-promoting factor Bud6.,Tu D, Graziano BR, Park E, Zheng W, Li Y, Goode BL, Eck MJ Proc Natl Acad Sci U S A. 2012 Nov 16. PMID:23161908<ref>PMID:23161908</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 3onx" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 18824]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Eck, M J]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Tu, D]]
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[[Category: Eck MJ]]
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[[Category: Coiled-coil]]
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[[Category: Tu D]]
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[[Category: Protein binding]]
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Revision as of 11:17, 21 February 2024

Crystal structure of a domain of a protein involved in formation of actin cytoskeleton

PDB ID 3onx

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