3sjh

<StructureSection load='3sjh' size='340' side='right' caption='[[3sjh]], [[Resolution|resolution]] 1.75&Aring;' scene=''>

<table><tr><td colspan='2'>[[3sjh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome] 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>

</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>

<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 DROME])</td></tr>

<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://pdbe.org/3sjh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3sjh RCSB], [http://www.ebi.ac.uk/pdbsum/3sjh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3sjh ProSAT]</span></td></tr>

[[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.

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.

 

== References ==

[[Category: Drome]]

[[Category: Carlier, M F]]

[[Category: Didry, D]]

[[Category: Husson, C]]

[[Category: Renault, L]]

[[Category: Protein-protein complex]]