The crystal structure of bacteriophage GA and a comparison of bacteriophages belonging to the major groups of Escherichia coli leviviruses
Identifieur interne : 003D13 ( Main/Exploration ); précédent : 003D12; suivant : 003D14The crystal structure of bacteriophage GA and a comparison of bacteriophages belonging to the major groups of Escherichia coli leviviruses
Auteurs : Kaspars Tars [Lettonie] ; Maija Bundule [Lettonie] ; Kerstin Fridborg [Suède] ; Lars Liljas [Suède]Source :
- Journal of Molecular Biology [ 0022-2836 ] ; 1997.
English descriptors
- KwdEn :
- GA, MS2, Qβ, virus assembly, virus evolution.
- Teeft :
- Academic press, Acid residues, Adenine bases, Amino, Amino acid residues, Amino acid sequence, Ammonium sulphate, Arginine residues, Assembly intermediates, Assembly pathway, Bacteriophage, Binding site, Binding sites, Biol, Capsid, Capsid formation, Capsid structure, Coat protein, Coat protein dimer, Coat protein gene, Coat protein mutants, Coat proteins, Cold spring harbor, Cold spring harbor laboratory press, Coliphage, Conformation, Crystal structure, Data collection, Different conformations, Dimer, Dimer crystal structure, Disulphide bridges, Electron density, Extra residue, Glycine residues, Golmohammadi, Helix, Hohn, Hydrogen bond, Hydrogen bonds, Hydrophobic, Hydrophobic core, Hydrophobic interactions, Icosahedral, Independent subunits, Individual subunits, Inner surface, Interaction, Interdimer interactions, Liljas, Loop conformations, Loop regions, Molecular replacement, Monomer, Mutant, Mutation, Mutation experiments, Outer surface, Particle assembly, Peabody, Pentamers, Phage, Phage particles, Phosphate groups, Plenum publishing corporation, Polar interactions, Proline residue, Protein shells, Replicase gene, Residue, Same orientation, Secondary structure elements, Sequence similarities, Stereo view, Stockley, Stonehouse, Subunit, Terminus, Trans conformation, Uhlenbeck, Valegard, Viral, Virus assembly.
Abstract
Abstract: The three-dimensional structure of the small T = 3 RNA bacteriophage GA has been determined at 3.4 Å resolution. The structure was solved by molecular replacement, using the phage MS2 as an initial model. A comparison of the protein shells of the four related phages GA, MS2, fr and Qβ was carried out in order to define structural features of particular importance for their assembly and specific RNA interaction. A high degree of similarity was found in the RNA binding sites, whereas larger structural differences are located in the loop regions of the coat proteins, especially in the FG loops forming 5-fold and quasi-6-fold contacts. The overall arrangement of the protein subunits in the shells of these phages is very similar, although the details of the interactions differ. The few conserved interactions are suggested to govern the subunit packing during assembly.
Url:
DOI: 10.1006/jmbi.1997.1214
Affiliations:
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type="ISSN">0022-2836</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>GA</term><term>MS2</term><term>Qβ</term><term>virus assembly</term><term>virus evolution</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Academic press</term><term>Acid residues</term><term>Adenine bases</term><term>Amino</term><term>Amino acid residues</term><term>Amino acid sequence</term><term>Ammonium sulphate</term><term>Arginine residues</term><term>Assembly intermediates</term><term>Assembly pathway</term><term>Bacteriophage</term><term>Binding site</term><term>Binding sites</term><term>Biol</term><term>Capsid</term><term>Capsid formation</term><term>Capsid structure</term><term>Coat protein</term><term>Coat protein dimer</term><term>Coat protein gene</term><term>Coat protein mutants</term><term>Coat proteins</term><term>Cold spring harbor</term><term>Cold spring harbor laboratory press</term><term>Coliphage</term><term>Conformation</term><term>Crystal structure</term><term>Data collection</term><term>Different conformations</term><term>Dimer</term><term>Dimer crystal structure</term><term>Disulphide bridges</term><term>Electron density</term><term>Extra residue</term><term>Glycine residues</term><term>Golmohammadi</term><term>Helix</term><term>Hohn</term><term>Hydrogen bond</term><term>Hydrogen bonds</term><term>Hydrophobic</term><term>Hydrophobic core</term><term>Hydrophobic interactions</term><term>Icosahedral</term><term>Independent subunits</term><term>Individual subunits</term><term>Inner surface</term><term>Interaction</term><term>Interdimer interactions</term><term>Liljas</term><term>Loop conformations</term><term>Loop regions</term><term>Molecular replacement</term><term>Monomer</term><term>Mutant</term><term>Mutation</term><term>Mutation experiments</term><term>Outer surface</term><term>Particle assembly</term><term>Peabody</term><term>Pentamers</term><term>Phage</term><term>Phage particles</term><term>Phosphate groups</term><term>Plenum publishing corporation</term><term>Polar interactions</term><term>Proline residue</term><term>Protein shells</term><term>Replicase gene</term><term>Residue</term><term>Same orientation</term><term>Secondary structure elements</term><term>Sequence similarities</term><term>Stereo view</term><term>Stockley</term><term>Stonehouse</term><term>Subunit</term><term>Terminus</term><term>Trans conformation</term><term>Uhlenbeck</term><term>Valegard</term><term>Viral</term><term>Virus assembly</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The three-dimensional structure of the small T = 3 RNA bacteriophage GA has been determined at 3.4 Å resolution. The structure was solved by molecular replacement, using the phage MS2 as an initial model. A comparison of the protein shells of the four related phages GA, MS2, fr and Qβ was carried out in order to define structural features of particular importance for their assembly and specific RNA interaction. A high degree of similarity was found in the RNA binding sites, whereas larger structural differences are located in the loop regions of the coat proteins, especially in the FG loops forming 5-fold and quasi-6-fold contacts. The overall arrangement of the protein subunits in the shells of these phages is very similar, although the details of the interactions differ. 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