2tmv

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Template:STRUCTURE 2tmv

Contents

VISUALIZATION OF PROTEIN-NUCLEIC ACID INTERACTIONS IN A VIRUS. REFINED STRUCTURE OF INTACT TOBACCO MOSAIC VIRUS AT 2.9 ANGSTROMS RESOLUTION BY X-RAY FIBER DIFFRACTION

Publication Abstract from PubMed

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.

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., Namba K, Pattanayek R, Stubbs G, J Mol Biol. 1989 Jul 20;208(2):307-25. PMID:2769760

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

2tmv is a 2 chain structure of Tobacco Mosaic Virus with sequence from Tobacco mosaic virus. The January 2009 RCSB PDB Molecule of the Month feature on Tobacco Mosaic Virus by David Goodsell is 10.2210/rcsb_pdb/mom_2009_1. Full crystallographic information is available from OCA.

See Also

Reference

  • Namba K, Pattanayek R, Stubbs G. 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. J Mol Biol. 1989 Jul 20;208(2):307-25. PMID:2769760
  • Parker MH, Hefford MA. A consensus residue analysis of loop and helix-capping residues in four-alpha-helical-bundle proteins. Protein Eng. 1997 May;10(5):487-96. PMID:9215566

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