CRYSTAL-STRUCTURE OF BACTERIOPHAGE-FR CAPSIDS AT 3.5-ANGSTROM RESOLUTION

被引：45

作者：

LILJAS, L ^{[1
]}

FRIDBORG, K ^{[1
]}

VALEGARD, K ^{[1
]}

BUNDULE, M ^{[1
]}

PUMPENS, P ^{[1
]}

机构：

[1] UNIV LATVIA,INST MOLEC BIOL,CTR BIOMED RES & STUDY,RIGA 1067,LATVIA

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1994年 / 244卷 / 03期

关键词：

PHAGE FR; PHAGE MS2; CRYSTAL STRUCTURE; VIRUS ASSEMBLY;

D O I：

10.1006/jmbi.1994.1729

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：

The structure of recombinant capsids of the bacterial virus fr has been determined by X-ray crystallography at 3.5 Angstrom resolution. The capsids were produced by expressing the fr coat protein in Escherichia coli, the natural host of the virus, and are probably essentially identical to the protein shell of the native virus. The structure was determined using molecular replacement with the protein shell of the related MS2 virus, and refined to a crystallographic R-factor of 0.228. A comparison of the protein shells of the viruses shows that they are very similar, and indicates that they may have a similar regulation of the assembly of the quasi-symmetrical protein shell.

引用

页码：279 / 290

页数：12

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