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Visualization of protein-nucleic acid interactions in a virus. Refined structure of intact tobacco mosaic virus at 2.9 A resolution by X-ray fiber diffraction.

Abstract：

:The structure of tobacco mosaic virus (TMV) has been determined by fiber diffraction methods at 2.9 A resolution, and refined by restrained least-squares to an R-factor of 0.096. Protein-nucleic acid interactions are clearly visible. The final model contains all of the non-hydrogen atoms of the RNA and the protein, 71 water molecules, and two calcium-binding sites. Viral disassembly is driven by electrostatic repulsions between the charges in two carboxyl-carboxylate pairs and a phosphate-carboxylate pair. The phosphate-carboxylate pair and at least one of the carboxyl-carboxylate pairs appear to be calcium-binding sites. Nucleotide specificity, enabling TMV to recognize its own RNA by a repeating pattern of guanine residues, is provided by two guanine-specific hydrogen bonds in one of the three base-binding sites.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Namba K,Pattanayek R,Stubbs G

doi

10.1016/0022-2836(89)90391-4

subject

Has Abstract

pub_date

1989-07-20 00:00:00

pages

307-25

issue

2

eissn

0022-2836

issn

1089-8638

pii

0022-2836(89)90391-4

journal_volume

208

pub_type

杂志文章

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