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Crystallization and preliminary X-Ray diffraction analysis of the 190-A-long coiled-coil dimerization domain of the actin-bundling protein cortexillin I from dictyostelium discoideum

Burkhard, P. and Steinmetz, M. O. and Schulthess, T. and Landwehr, R. and Aebi, U. and Kammerer, R. A.. (1998) Crystallization and preliminary X-Ray diffraction analysis of the 190-A-long coiled-coil dimerization domain of the actin-bundling protein cortexillin I from dictyostelium discoideum. Journal of Structural Biology, Vol. 122, H. 3. pp. 293-296.

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Official URL: http://edoc.unibas.ch/dok/A5258527

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Abstract

We have crystallized the approximately 190-A-long parallel two-stranded coiled-coil oligomerization domain of the actin-bundling protein cortexillin I from Dictyostelium discoideum. The orthorhombic crystals belong to the space group C2221 with unit cell dimensions of a = 71.3 A, b = 127.8 A, and c = 91.6 A. As both native and selenomethionine-substituted protein crystals diffract to 3.0 and 2.85 A resolution, respectively, using synchrotron radiation, they are suitable for the first high-resolution structural analysis of a two-stranded coiled coil comprising more than six heptad repeats. Moreover, because the polypeptide chain fragment contains a recently identified two-heptad-repeat long sequence that is indispensable for the assembly of the cortexillin I coiled-coil oligomerization domain, its high-resolution structure should enable us to extend our knowledge on the molecular mechanisms underlaying coiled-coil formation and to establish the precise manner in which the two "trigger" sequences interact with one another in the dimer.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology, associated group (Burkhard)
UniBasel Contributors:Burkhard, Peter
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Academic Press
ISSN:1047-8477
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:22 Mar 2012 14:20
Deposited On:22 Mar 2012 13:20

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