1sqk
From Proteopedia
(New page: 200px<br /><applet load="1sqk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sqk, resolution 2.50Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1sqk.gif|left|200px]]<br /><applet load="1sqk" size=" | + | [[Image:1sqk.gif|left|200px]]<br /><applet load="1sqk" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1sqk, resolution 2.50Å" /> | caption="1sqk, resolution 2.50Å" /> | ||
'''CRYSTAL STRUCTURE OF CIBOULOT IN COMPLEX WITH SKELETAL ACTIN'''<br /> | '''CRYSTAL STRUCTURE OF CIBOULOT IN COMPLEX WITH SKELETAL ACTIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The widespread beta-thymosin/WH2 actin binding domain has versatile | + | 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== | ==About this Structure== | ||
| - | 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 MG, ADP and LAR as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Carlier, M | + | [[Category: Carlier, M F.]] |
[[Category: Coutant, J.]] | [[Category: Coutant, J.]] | ||
[[Category: Didelot, G.]] | [[Category: Didelot, G.]] | ||
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[[Category: Gigant, B.]] | [[Category: Gigant, B.]] | ||
[[Category: Guittet, E.]] | [[Category: Guittet, E.]] | ||
| - | [[Category: Heijenoort, C | + | [[Category: Heijenoort, C Van.]] |
[[Category: Hertzog, M.]] | [[Category: Hertzog, M.]] | ||
[[Category: Knossow, M.]] | [[Category: Knossow, M.]] | ||
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[[Category: ciboulot; wh2 domain; actin; actin-binding protein]] | [[Category: ciboulot; wh2 domain; actin; actin-binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:04:13 2008'' |
Revision as of 13:04, 21 February 2008
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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 with , and as ligands. 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 Thu Feb 21 15:04:13 2008
Categories: Drosophila melanogaster | Oryctolagus cuniculus | Protein complex | Carlier, M F. | Coutant, J. | Didelot, G. | Didry, D. | Gaudier, M. | Gigant, B. | Guittet, E. | Heijenoort, C Van. | Hertzog, M. | Knossow, M. | Preat, T. | ADP | LAR | MG | Ciboulot; wh2 domain; actin; actin-binding protein
