1tx9
From Proteopedia
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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 Wed Nov 21 03:39:52 2007
