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1CD3

PROCAPSID OF BACTERIOPHAGE PHIX174

Summary for 1CD3
Entry DOI10.2210/pdb1cd3/pdb
DescriptorPROTEIN (SCAFFOLDING PROTEIN GPD), PROTEIN (CAPSID PROTEIN GPF), PROTEIN (SPIKE PROTEIN GPG), ... (5 entities in total)
Functional Keywordscomplex (virus capsid proteins), bacteriophage, procapsid, scaffolding protein, chaperone, icosahedral virus, virus
Biological sourceEnterobacteria phage phiX174
More
Total number of polymer chains7
Total formula weight149145.41
Authors
Rossmann, M.G.,Dokland, T. (deposition date: 1999-03-05, release date: 1999-04-14, Last modification date: 2024-04-03)
Primary citationDokland, T.,Bernal, R.A.,Burch, A.,Pletnev, S.,Fane, B.A.,Rossmann, M.G.
The role of scaffolding proteins in the assembly of the small, single-stranded DNA virus phiX174.
J.Mol.Biol., 288:595-608, 1999
Cited by
PubMed Abstract: An empty precursor particle called the procapsid is formed during assembly of the single-stranded DNA bacteriophage phiX174. Assembly of the phiX174 procapsid requires the presence of the two scaffolding proteins, D and B, which are structural components of the procapsid, but are not found in the mature virion. The X-ray crystallographic structure of a "closed" procapsid particle has been determined to 3.5 A resolution. This structure has an external scaffold made from 240 copies of protein D, 60 copies of the internally located B protein, and contains 60 copies of each of the viral structural proteins F and G, which comprise the shell and the 5-fold spikes, respectively. The F capsid protein has a similar conformation to that seen in the mature virion, and differs from the previously determined 25 A resolution electron microscopic reconstruction of the "open" procapsid, in which the F protein has a different conformation. The D scaffolding protein has a predominantly alpha-helical fold and displays remarkable conformational variability. We report here an improved and refined structure of the closed procapsid and describe in some detail the differences between the four independent D scaffolding proteins per icosahedral asymmetric unit, as well as their interaction with the F capsid protein. We re-analyze and correct the comparison of the closed procapsid with the previously determined cryo-electron microscopic image reconstruction of the open procapsid and discuss the major structural rearrangements that must occur during assembly. A model is proposed in which the D proteins direct the assembly process by sequential binding and conformational switching.
PubMed: 10329166
DOI: 10.1006/jmbi.1999.2699
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.5 Å)
Structure validation

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