Conformational switching by the scaffolding protein D directs the assembly of bacteriophage phiX174 |
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Authors: | Morais Marc C Fisher Megan Kanamaru Shuji Przybyla Laralynne Burgner John Fane Bentley A Rossmann Michael G |
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Institution: | Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, IN 47907, USA. |
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Abstract: | The three-dimensional structure of bacteriophage phiX174 external scaffolding protein D, prior to its interaction with other structural proteins, has been determined to 3.3 angstroms by X-ray crystallography. The crystals belong to space group P4(1)2(1)2 with a dimer in the asymmetric unit that closely resembles asymmetric dimers observed in the phiX174 procapsid structure. Furthermore, application of the crystallographic 4(1) symmetry operation to one of these dimers generates a tetramer similar to the tetramer in the icosahedral asymmetric unit of the procapsid. These data suggest that both dimers and tetramers of the D protein are true morphogenetic intermediates and can form independently of other proteins involved in procapsid morphogenesis. The crystal structure of the D scaffolding protein thus represents the state of the polypeptide prior to procapsid assembly. Hence, comparison with the procapsid structure provides a rare opportunity to follow the conformational switching events necessary for the construction of complex macromolecular assemblies. |
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