3onx

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[[Image:3onx.png|left|200px]]
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==Crystal structure of a domain of a protein involved in formation of actin cytoskeleton==
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<StructureSection load='3onx' size='340' side='right' caption='[[3onx]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3onx]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3okq|3okq]]</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 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3onx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3onx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3onx RCSB], [http://www.ebi.ac.uk/pdbsum/3onx PDBsum]</span></td></tr>
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</table>
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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_3onx| PDB=3onx | SCENE= }}
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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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===Crystal structure of a domain of a protein involved in formation of actin cytoskeleton===
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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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{{ABSTRACT_PUBMED_23161908}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[3onx]] is a 2 chain structure with sequence from [http://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].
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</StructureSection>
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Eck, M J.]]
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[[Category: Eck, M J]]
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[[Category: Tu, D.]]
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[[Category: Tu, D]]
[[Category: Coiled-coil]]
[[Category: Coiled-coil]]
[[Category: Protein binding]]
[[Category: Protein binding]]

Revision as of 12:48, 9 December 2014

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

3onx, resolution 2.90Å

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