STRUCTURES OF THE HELICAL AGGREGATES OF TOBACCO MOSAIC-VIRUS PROTEIN

被引：33

作者：

MANDELKOW, E

STUBBS, G

WARREN, S

机构：

[1] BRANDEIS UNIV, ROSENSTIEL BASIC MED SCI RES CTR, WALTHAM, MA 02154 USA

[2] MAX PLANCK INST MED RES, DEPT BIOPHYS, D-6900 HEIDELBERG, FED REP GER

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1981年 / 152卷 / 02期

关键词：

D O I：

10.1016/0022-2836(81)90248-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Tobacco mosaic virus coat protein forms 2 helical aggregates, with 161/3 and 17 1/3 subunits/turn. Both were studied and compared with the intact virus by recording X-ray diffraction from oriented gels and calculating difference Fourier maps. The protein forms have structures similar to each other and to the protein part of the virus, even in the low radius region, which has a different structure in the crystalline disk form of the protein. The RNA is replaced in the helical protein forms by at least 1 bound anion. The difference between the protein forms may possibly be related to the conformation of 1 or more of the arginine groups that bind RNA in the intact virus.

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页码：375 / 386

页数：12

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