3u9d

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
{{STRUCTURE_3u9d| PDB=3u9d | SCENE= }}
+
==Crystal Structure of a chimera containing the N-terminal domain (residues 8-24) of drosophila Ciboulot and the C-terminal domain (residues 13-44) of bovine Thymosin-beta4, bound to G-actin-ATP==
-
===Crystal Structure of a chimera containing the N-terminal domain (residues 8-24) of drosophila Ciboulot and the C-terminal domain (residues 13-44) of bovine Thymosin-beta4, bound to G-actin-ATP===
+
<StructureSection load='3u9d' size='340' side='right' caption='[[3u9d]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-
{{ABSTRACT_PUBMED_22193718}}
+
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3u9d]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U9D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U9D 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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 +
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sjh|3sjh]], [[3u8x|3u8x]], [[1sqk|1sqk]], [[3u9z|3u9z]]</td></tr>
 +
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TMSB4, THYB4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus])</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=3u9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u9d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u9d RCSB], [http://www.ebi.ac.uk/pdbsum/3u9d PDBsum]</span></td></tr>
 +
</table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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.
-
==Function==
+
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>
-
[[http://www.uniprot.org/uniprot/ACTS_RAT ACTS_RAT]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [[http://www.uniprot.org/uniprot/TYB4_BOVIN TYB4_BOVIN]] Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization (By similarity). Seraspenide inhibits the entry of hematopoietic pluripotent stem cells into the S-phase.
+
-
==About this Structure==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[3u9d]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U9D OCA].
+
</div>
==See Also==
==See Also==
*[[Actin|Actin]]
*[[Actin|Actin]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:022193718</ref><references group="xtra"/><references/>
+
__TOC__
 +
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
-
[[Category: Carlier, M F.]]
+
[[Category: Carlier, M F]]
-
[[Category: Didry, D.]]
+
[[Category: Didry, D]]
-
[[Category: Husson, C.]]
+
[[Category: Husson, C]]
-
[[Category: Renault, L.]]
+
[[Category: Renault, L]]
[[Category: Contractile protein]]
[[Category: Contractile protein]]
[[Category: Protein binding]]
[[Category: Protein binding]]

Revision as of 07:16, 21 December 2014

Crystal Structure of a chimera containing the N-terminal domain (residues 8-24) of drosophila Ciboulot and the C-terminal domain (residues 13-44) of bovine Thymosin-beta4, bound to G-actin-ATP

3u9d, resolution 2.50Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3u9d"
Personal tools