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1W8X

Structural analysis of PRD1

Summary for 1W8X
Entry DOI10.2210/pdb1w8x/pdb
Related1CJD 1GW7 1GW8 1HB5 1HB7 1HB9 1HQN 1HX6
DescriptorMAJOR CAPSID PROTEIN (PROTEIN P3), PROTEIN P30, PROTEIN P31, ... (4 entities in total)
Functional Keywordsvirus, p3 major capsid protein, p30 tape measure, p31 penton protein, p16 membrane protein, virus/viral protein, icosahedral virus
Biological sourceENTEROBACTERIA PHAGE PRD1
More
Cellular locationVirion: P22535 P27391 P27384
Virion membrane ; Single-pass membrane protein : P27392
Total number of polymer chains15
Total formula weight557106.82
Authors
Primary citationAbrescia, N.G.A.,Cockburn, J.J.B.,Grimes, J.M.,Sutton, G.C.,Diprose, J.M.,Butcher, S.J.,Fuller, S.D.,San Martin, C.,Burnett, R.M.,Stuart, D.I.,Bamford, D.H.,Bamford, J.K.H.
Insights Into Assembly from Structural Analysis of Bacteriophage Prd1.
Nature, 432:68-, 2004
Cited by
PubMed Abstract: The structure of the membrane-containing bacteriophage PRD1 has been determined by X-ray crystallography at about 4 A resolution. Here we describe the structure and location of proteins P3, P16, P30 and P31. Different structural proteins seem to have specialist roles in controlling virus assembly. The linearly extended P30 appears to nucleate the formation of the icosahedral facets (composed of trimers of the major capsid protein, P3) and acts as a molecular tape-measure, defining the size of the virus and cementing the facets together. Pentamers of P31 form the vertex base, interlocking with subunits of P3 and interacting with the membrane protein P16. The architectural similarities with adenovirus and one of the largest known virus particles PBCV-1 support the notion that the mechanism of assembly of PRD1 is scaleable and applies across the major viral lineage formed by these viruses.
PubMed: 15525981
DOI: 10.1038/NATURE03056
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (4.2 Å)
Structure validation

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건을2024-11-06부터공개중

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