3sjh

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{{STRUCTURE_3sjh| PDB=3sjh | SCENE= }}
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==Crystal Structure of a chimera containing the N-terminal domain (residues 8-29) of drosophila Ciboulot and the C-terminal domain (residues 18-44) of bovine Thymosin-beta4, bound to G-actin-ATP-Latrunculin A==
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===Crystal Structure of a chimera containing the N-terminal domain (residues 8-29) of drosophila Ciboulot and the C-terminal domain (residues 18-44) of bovine Thymosin-beta4, bound to G-actin-ATP-Latrunculin A===
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<StructureSection load='3sjh' size='340' side='right' caption='[[3sjh]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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{{ABSTRACT_PUBMED_22193718}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3sjh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] 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=3SJH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SJH 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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=LAR:LATRUNCULIN+A'>LAR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=9913 Bos taurus])</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=3sjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sjh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sjh RCSB], [http://www.ebi.ac.uk/pdbsum/3sjh 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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[[3sjh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] 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=3SJH 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: Bos taurus]]
[[Category: Bos taurus]]
[[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]]
[[Category: Protein-protein complex]]
[[Category: Protein-protein complex]]

Revision as of 07:32, 21 December 2014

Crystal Structure of a chimera containing the N-terminal domain (residues 8-29) of drosophila Ciboulot and the C-terminal domain (residues 18-44) of bovine Thymosin-beta4, bound to G-actin-ATP-Latrunculin A

3sjh, resolution 1.75Å

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