1cd3: Difference between revisions
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{{STRUCTURE_1cd3| PDB=1cd3 | SCENE= }} | |||
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'''PROCAPSID OF BACTERIOPHAGE PHIX174''' | '''PROCAPSID OF BACTERIOPHAGE PHIX174''' | ||
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[[Category: Dokland, T.]] | [[Category: Dokland, T.]] | ||
[[Category: Rossmann, M G.]] | [[Category: Rossmann, M G.]] | ||
[[Category: | [[Category: Bacteriophage]] | ||
[[Category: | [[Category: Chaperone]] | ||
[[Category: | [[Category: Icosahedral virus]] | ||
[[Category: | [[Category: Procapsid]] | ||
[[Category: | [[Category: Scaffolding protein]] | ||
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Revision as of 12:35, 2 May 2008
PROCAPSID OF BACTERIOPHAGE PHIX174
OverviewOverview
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.
About this StructureAbout this Structure
1CD3 is a Protein complex structure of sequences from Enterobacteria phage phix174. The following page contains interesting information on the relation of 1CD3 with [Bacteriophage phiX174]. Full crystallographic information is available from OCA.
ReferenceReference
The role of scaffolding proteins in the assembly of the small, single-stranded DNA virus phiX174., Dokland T, Bernal RA, Burch A, Pletnev S, Fane BA, Rossmann MG, J Mol Biol. 1999 May 14;288(4):595-608. PMID:10329166 Page seeded by OCA on Fri May 2 12:35:57 2008