1hb9: Difference between revisions
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'''QUASI-ATOMIC RESOLUTION MODEL OF BACTERIOPHAGE PRD1 WILD TYPE VIRION, OBTAINED BY COMBINED CRYO-EM AND X-RAY CRYSTALLOGRAPHY.''' | '''QUASI-ATOMIC RESOLUTION MODEL OF BACTERIOPHAGE PRD1 WILD TYPE VIRION, OBTAINED BY COMBINED CRYO-EM AND X-RAY CRYSTALLOGRAPHY.''' | ||
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[[Category: Martin, C San.]] | [[Category: Martin, C San.]] | ||
[[Category: Rutten, T.]] | [[Category: Rutten, T.]] | ||
[[Category: | [[Category: Bacteriophage prd1]] | ||
[[Category: | [[Category: Cryo-em]] | ||
[[Category: | [[Category: Icosahedral virus]] | ||
[[Category: | [[Category: Image reconstruction]] | ||
[[Category: | [[Category: Tectiviridae]] | ||
[[Category: | [[Category: Virus/viral protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:39:50 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 18:39, 2 May 2008
QUASI-ATOMIC RESOLUTION MODEL OF BACTERIOPHAGE PRD1 WILD TYPE VIRION, OBTAINED BY COMBINED CRYO-EM AND X-RAY CRYSTALLOGRAPHY.
OverviewOverview
BACKGROUND: The dsDNA bacteriophage PRD1 has a membrane inside its icosahedral capsid. While its large size (66 MDa) hinders the study of the complete virion at atomic resolution, a 1.65-A crystallographic structure of its major coat protein, P3, is available. Cryo-electron microscopy (cryo-EM) and three-dimensional reconstruction have shown the capsid at 20-28 A resolution. Striking architectural similarities between PRD1 and the mammalian adenovirus indicate a common ancestor. RESULTS: The P3 atomic structure has been fitted into improved cryo-EM reconstructions for three types of PRD1 particles: the wild-type virion, a packaging mutant without DNA, and a P3-shell lacking the membrane and the vertices. Establishing the absolute EM scale was crucial for an accurate match. The resulting "quasi-atomic" models of the capsid define the residues involved in the major P3 interactions, within the quasi-equivalent interfaces and with the membrane, and show how these are altered upon DNA packaging. CONCLUSIONS: The new cryo-EM reconstructions reveal the structure of the PRD1 vertex and the concentric packing of DNA. The capsid is essentially unchanged upon DNA packaging, with alterations limited to those P3 residues involved in membrane contacts. These are restricted to a few of the N termini along the icosahedral edges in the empty particle; DNA packaging leads to a 4-fold increase in the number of contacts, including almost all copies of the N terminus and the loop between the two beta barrels. Analysis of the P3 residues in each quasi-equivalent interface suggests two sites for minor proteins in the capsid edges, analogous to those in adenovirus.
About this StructureAbout this Structure
1HB9 is a Single protein structure of sequence from Enterobacteria phage prd1. Full crystallographic information is available from OCA.
ReferenceReference
Combined EM/X-ray imaging yields a quasi-atomic model of the adenovirus-related bacteriophage PRD1 and shows key capsid and membrane interactions., Martin CS, Burnett RM, de Haas F, Heinkel R, Rutten T, Fuller SD, Butcher SJ, Bamford DH, Structure. 2001 Oct;9(10):917-30. PMID:11591347 Page seeded by OCA on Fri May 2 18:39:50 2008