The structure of an infectious P22 virion shows the signal for headful DNA packaging

被引：250

作者：

Lander, Gabriel C.

Tang, Liang

Casjens, Sherwood R.

Gilcrease, Eddie B.

Prevelige, Peter

Poliakov, Anton

Potter, Clinton S.

Carragher, Bridget

Johnson, John E.

机构：

[1] Scripps Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA

[2] Scripps Res Inst, Dept Cell Biol, La Jolla, CA 92037 USA

[3] Univ Utah, Sch Med, Dept Pathol, Salt Lake City, UT 84112 USA

[4] Univ Alabama Birmingham, Dept Microbiol, Birmingham, AL 35294 USA

来源：

SCIENCE | 2006年 / 312卷 / 5781期

关键词：

D O I：

10.1126/science.1127981

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：

Bacteriophages, herpesviruses, and other large double-stranded DNA (dsDNA) viruses contain molecular machines that pump DNA into preassembled procapsids, generating internal capsid pressures exceeding, by 10-fold, that of bottled champagne. A 17 angstrom resolution asymmetric reconstruction of the infectious P22 virion reveals that tightly spooled DNA about the portal dodecamer forces a conformation that is significantly different from that observed in isolated portals assembled from ectopically expressed protein. We propose that the tight dsDNA spooling activates the switch that signals the headful chromosome packing density to the particle exterior.

引用

页码：1791 / 1795

页数：5

共 23 条

[21] Phage P22 tailspike protein: Crystal structure of the head-binding domain at 2.3 angstrom, fully refined structure of the endorhamnosidase at 1.56 angstrom resolution, and the molecular basis of O-antigen recognition and cleavage [J].