1tx9: Difference between revisions
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'''gpd prior to capsid assembly''' | '''gpd prior to capsid assembly''' | ||
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[[Category: Morais, M C.]] | [[Category: Morais, M C.]] | ||
[[Category: Rossmann, M G.]] | [[Category: Rossmann, M G.]] | ||
[[Category: | [[Category: Assembly]] | ||
[[Category: | [[Category: Conformational switching]] | ||
[[Category: | [[Category: Phix174]] | ||
[[Category: | [[Category: Scaffolding protein]] | ||
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Revision as of 07:28, 3 May 2008
gpd prior to capsid assembly
Overview
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.
About this Structure
1TX9 is a Single protein structure of sequence from Enterobacteria phage phix174. Full crystallographic information is available from OCA.
Reference
Conformational switching by the scaffolding protein D directs the assembly of bacteriophage phiX174., Morais MC, Fisher M, Kanamaru S, Przybyla L, Burgner J, Fane BA, Rossmann MG, Mol Cell. 2004 Sep 24;15(6):991-7. PMID:15383287 Page seeded by OCA on Sat May 3 10:28:50 2008
