1sqk

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[[Image:1sqk.gif|left|200px]]<br /><applet load="1sqk" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1sqk.gif|left|200px]]
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caption="1sqk, resolution 2.50&Aring;" />
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'''CRYSTAL STRUCTURE OF CIBOULOT IN COMPLEX WITH SKELETAL ACTIN'''<br />
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{{Structure
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|PDB= 1sqk |SIZE=350|CAPTION= <scene name='initialview01'>1sqk</scene>, resolution 2.50&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=LAR:LATRUNCULIN A'>LAR</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF CIBOULOT IN COMPLEX WITH SKELETAL ACTIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1SQK is a [http://en.wikipedia.org/wiki/Protein_complex 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] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ADP:'>ADP</scene> and <scene name='pdbligand=LAR:'>LAR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SQK OCA].
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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==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15163409 15163409]
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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: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: ciboulot; wh2 domain; actin; actin-binding protein]]
[[Category: ciboulot; wh2 domain; actin; actin-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:04:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:08:23 2008''

Revision as of 12:08, 20 March 2008

Image:1sqk.gif


PDB ID 1sqk

Drag the structure with the mouse to rotate
, resolution 2.50Å
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF CIBOULOT IN COMPLEX WITH SKELETAL ACTIN


Overview

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.

About this Structure

1SQK is a Protein complex structure of sequences from Drosophila melanogaster and Oryctolagus cuniculus. Full crystallographic information is available from 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:15163409

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