Insights into assembly from structural analysis of bacteriophage PRD1

被引：208

作者：

Abrescia, NGA

Cockburn, JJB

Grimes, JM

Sutton, GC

Diprose, JM

Butcher, SJ

Fuller, SD

Martín, CS

Burnett, RM

Stuart, DI

Bamford, DH

Bamford, JKH

机构：

[1] Univ Oxford, Wellcome Trust Ctr Human Genet, Div Struct Biol, Oxford OX3 7BN, England

[2] Univ Oxford, Cent Chem Lab, Oxford Ctr Mol Sci, Oxford OX1 3QT, England

[3] Univ Helsinki, Inst Biotechnol, Viikinkaari 5 00014, Finland

[4] Univ Helsinki, Fac Biosci, Viikki Bioctr, Viikinkaari 5 00014, Finland

[5] Wistar Inst Anat & Biol, Philadelphia, PA 19104 USA

来源：

NATURE | 2004年 / 432卷 / 7013期

基金：

英国惠康基金; 芬兰科学院; 英国生物技术与生命科学研究理事会; 美国国家科学基金会; 英国医学研究理事会;

关键词：

D O I：

10.1038/nature03056

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The structure of the membrane-containing bacteriophage PRD1 has been determined by X-ray crystallography at about 4 Angstrom 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.

引用

页码：68 / 74

页数：7

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