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{{Seed}}
[[Image:1sqk.png|left|200px]]


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==CRYSTAL STRUCTURE OF CIBOULOT IN COMPLEX WITH SKELETAL ACTIN==
The line below this paragraph, containing "STRUCTURE_1sqk", creates the "Structure Box" on the page.
<StructureSection load='1sqk' size='340' side='right'caption='[[1sqk]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1sqk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SQK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SQK FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=LAR:LATRUNCULIN+A'>LAR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
{{STRUCTURE_1sqk|  PDB=1sqk  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sqk OCA], [https://pdbe.org/1sqk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sqk RCSB], [https://www.ebi.ac.uk/pdbsum/1sqk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sqk ProSAT]</span></td></tr>
</table>
== Function ==
[https://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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The widespread beta-thymosin/WH2 actin binding domain has versatile regulatory properties in actin dynamics and motility. beta-thymosins (isolated WH2 domain) maintain monomeric actin in a "sequestered" nonpolymerizable form. In contrast, when repeated in tandem or inserted in modular proteins, the beta-thymosin/WH2 domain promotes actin assembly at filament barbed ends, like profilin. The structural basis for these opposite functions is addressed using ciboulot, a three beta-thymosin repeat protein. Only the first repeat binds actin and possesses the function of ciboulot. The region that shows the strongest interaction with actin is an amphipathic N-terminal alpha helix, present in all beta-thymosin/WH2 domains, which recognizes the ATP bound actin structure and uses the shear motion of actin linked to ATP hydrolysis to control polymerization. Crystallographic ((1)H, (15)N), NMR, and mutagenetic data reveal that the weaker interaction of the C-terminal region of beta-thymosin/WH2 domain with actin accounts for the switch in function from inhibition to promotion of actin assembly.


===CRYSTAL STRUCTURE OF CIBOULOT IN COMPLEX WITH SKELETAL ACTIN===
The beta-thymosin/WH2 domain; structural basis for the switch from inhibition to promotion of actin assembly.,Hertzog M, van Heijenoort C, Didry D, Gaudier M, Coutant J, Gigant B, Didelot G, Preat T, Knossow M, Guittet E, Carlier MF Cell. 2004 May 28;117(5):611-23. PMID:15163409<ref>PMID:15163409</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1sqk" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_15163409}}, adds the Publication Abstract to the page
*[[Actin 3D structures|Actin 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 15163409 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_15163409}}
__TOC__
 
</StructureSection>
==About this Structure==
1SQK is a [[Protein complex]] structure of sequences 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=1SQK OCA].
 
==Reference==
The beta-thymosin/WH2 domain; structural basis for the switch from inhibition to promotion of actin assembly., Hertzog M, van Heijenoort C, Didry D, Gaudier M, Coutant J, Gigant B, Didelot G, Preat T, Knossow M, Guittet E, Carlier MF, Cell. 2004 May 28;117(5):611-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15163409 15163409]
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Protein complex]]
[[Category: Carlier MF]]
[[Category: Carlier, M F.]]
[[Category: Coutant J]]
[[Category: Coutant, J.]]
[[Category: Didelot G]]
[[Category: Didelot, G.]]
[[Category: Didry D]]
[[Category: Didry, D.]]
[[Category: Gaudier M]]
[[Category: Gaudier, M.]]
[[Category: Gigant B]]
[[Category: Gigant, B.]]
[[Category: Guittet E]]
[[Category: Guittet, E.]]
[[Category: Hertzog M]]
[[Category: Heijenoort, C Van.]]
[[Category: Knossow M]]
[[Category: Hertzog, M.]]
[[Category: Preat T]]
[[Category: Knossow, M.]]
[[Category: Van Heijenoort C]]
[[Category: Preat, T.]]
[[Category: Actin]]
[[Category: Actin-binding protein]]
[[Category: Ciboulot]]
[[Category: Wh2 domain]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:57:08 2008''

Latest revision as of 00:36, 29 June 2023

CRYSTAL STRUCTURE OF CIBOULOT IN COMPLEX WITH SKELETAL ACTINCRYSTAL STRUCTURE OF CIBOULOT IN COMPLEX WITH SKELETAL ACTIN

Structural highlights

1sqk is a 2 chain structure with sequence from Drosophila melanogaster and Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ACTS_RABIT Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

Publication Abstract from PubMed

The widespread beta-thymosin/WH2 actin binding domain has versatile regulatory properties in actin dynamics and motility. beta-thymosins (isolated WH2 domain) maintain monomeric actin in a "sequestered" nonpolymerizable form. In contrast, when repeated in tandem or inserted in modular proteins, the beta-thymosin/WH2 domain promotes actin assembly at filament barbed ends, like profilin. The structural basis for these opposite functions is addressed using ciboulot, a three beta-thymosin repeat protein. Only the first repeat binds actin and possesses the function of ciboulot. The region that shows the strongest interaction with actin is an amphipathic N-terminal alpha helix, present in all beta-thymosin/WH2 domains, which recognizes the ATP bound actin structure and uses the shear motion of actin linked to ATP hydrolysis to control polymerization. Crystallographic ((1)H, (15)N), NMR, and mutagenetic data reveal that the weaker interaction of the C-terminal region of beta-thymosin/WH2 domain with actin accounts for the switch in function from inhibition to promotion of actin assembly.

The beta-thymosin/WH2 domain; structural basis for the switch from inhibition to promotion of actin assembly.,Hertzog M, van Heijenoort C, Didry D, Gaudier M, Coutant J, Gigant B, Didelot G, Preat T, Knossow M, Guittet E, Carlier MF Cell. 2004 May 28;117(5):611-23. PMID:15163409[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Hertzog M, van Heijenoort C, Didry D, Gaudier M, Coutant J, Gigant B, Didelot G, Preat T, Knossow M, Guittet E, Carlier MF. The beta-thymosin/WH2 domain; structural basis for the switch from inhibition to promotion of actin assembly. Cell. 2004 May 28;117(5):611-23. PMID:15163409

1sqk, resolution 2.50Å

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