1sqk
From Proteopedia
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|PDB= 1sqk |SIZE=350|CAPTION= <scene name='initialview01'>1sqk</scene>, resolution 2.50Å | |PDB= 1sqk |SIZE=350|CAPTION= <scene name='initialview01'>1sqk</scene>, resolution 2.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <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> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sqk OCA], [http://www.ebi.ac.uk/pdbsum/1sqk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sqk RCSB]</span> | ||
}} | }} | ||
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[[Category: Knossow, M.]] | [[Category: Knossow, M.]] | ||
[[Category: Preat, T.]] | [[Category: Preat, T.]] | ||
| - | [[Category: | + | [[Category: actin]] |
| - | [[Category: | + | [[Category: actin-binding protein]] |
| - | [[Category: | + | [[Category: ciboulot]] |
| - | [[Category: | + | [[Category: wh2 domain]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:45:42 2008'' |
Revision as of 20:45, 30 March 2008
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| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Sun Mar 30 23:45:42 2008
