3u9z

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{{STRUCTURE_3u9z| PDB=3u9z | SCENE= }}
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==Crystal structure between actin and a protein construct containing the first beta-thymosin domain of drosophila ciboulot (residues 2-58) with the three mutations N26D/Q27K/D28S==
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===Crystal structure between actin and a protein construct containing the first beta-thymosin domain of drosophila ciboulot (residues 2-58) with the three mutations N26D/Q27K/D28S===
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<StructureSection load='3u9z' size='340' side='right' caption='[[3u9z]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
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{{ABSTRACT_PUBMED_22193718}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3u9z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U9Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U9Z FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sjh|3sjh]], [[3u8x|3u8x]], [[3u9d|3u9d]], [[1sqk|1sqk]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cib, EG:EG0007.11, CG4944, Dmel_CG4944 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])</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=3u9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u9z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u9z RCSB], [http://www.ebi.ac.uk/pdbsum/3u9z 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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beta-Thymosin (betaT) and WH2 domains are widespread, intrinsically disordered actin-binding peptides that display significant sequence variability and different regulations of actin self-assembly in motile and morphogenetic processes. Here, we reveal the structural mechanisms by which, in their 1:1 stoichiometric complexes with actin, they either inhibit assembly by sequestering actin monomers like Thymosin-beta4, or enhance motility by directing polarized filament assembly like Ciboulot betaT. We combined mutational, functional or structural analysis by X-ray crystallography, SAXS (small angle X-ray scattering) and NMR on Thymosin-beta4, Ciboulot, TetraThymosinbeta and the long WH2 domain of WASP-interacting protein. The latter sequesters G-actin with the same molecular mechanisms as Thymosin-beta4. Functionally different betaT/WH2 domains differ by distinct dynamics of their C-terminal half interactions with G-actin pointed face. These C-terminal interaction dynamics are controlled by the strength of electrostatic interactions with G-actin. At physiological ionic strength, a single salt bridge with actin located next to their central LKKT/V motif induces G-actin sequestration in both isolated long betaT and WH2 domains. The results open perspectives for elucidating the functions of betaT/WH2 domains in other modular proteins.
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==Function==
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How a single residue in individual beta-thymosin/WH2 domains controls their functions in actin assembly.,Didry D, Cantrelle FX, Husson C, Roblin P, Moorthy AM, Perez J, Le Clainche C, Hertzog M, Guittet E, Carlier MF, van Heijenoort C, Renault L EMBO J. 2011 Dec 23. doi: 10.1038/emboj.2011.461. PMID:22193718<ref>PMID:22193718</ref>
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[[http://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT]] 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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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[3u9z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U9Z OCA].
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</div>
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==Reference==
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==See Also==
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<ref group="xtra">PMID:022193718</ref><references group="xtra"/><references/>
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*[[Actin|Actin]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Carlier, M F.]]
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[[Category: Carlier, M F]]
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[[Category: Didry, D.]]
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[[Category: Didry, D]]
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[[Category: Husson, C.]]
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[[Category: Husson, C]]
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[[Category: Renault, L.]]
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[[Category: Renault, L]]
[[Category: Contractile protein]]
[[Category: Contractile protein]]
[[Category: Protein binding]]
[[Category: Protein binding]]

Revision as of 07:05, 21 December 2014

Crystal structure between actin and a protein construct containing the first beta-thymosin domain of drosophila ciboulot (residues 2-58) with the three mutations N26D/Q27K/D28S

3u9z, resolution 2.09Å

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