1TX9

gpd prior to capsid assembly

Summary for 1TX9

• Entry DOI: 10.2210/pdb1tx9/pdb
• Related: 1CD3
• Descriptor: Scaffolding protein D (1 entity in total)
• Functional Keywords: scaffolding protein, phix174, assembly, conformational switching, structural protein
• Biological source: Enterobacteria phage phiX174
• Total number of polymer chains: 2
• Total formula weight: 33644.24

Authors

Morais, M.C.,Fisher, M.,Kanamaru, K.,Fane, B.A.,Rossmann, M.G. (deposition date: 2004-06-24, release date: 2005-04-26, Last modification date: 2023-08-23)

Primary citation

Morais, M.C.,Fisher, M.,Kanamaru, S.,Przybyla, L.,Burgner, J.,Fane, B.A.,Rossmann, M.G.
Conformational switching by the scaffolding protein D directs the assembly of bacteriophage phiX174
Mol.Cell, 15:991-997, 2004

PubMed 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.

PubMed: 15383287
DOI: 10.1016/j.molcel.2004.08.023

Experimental method

X-RAY DIFFRACTION (3.31 Å)