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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1994-1-12
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pubmed:abstractText |
Bacteriophage MS2 is an icosahedral virus with 180 copies of a coat protein forming a shell around a single-stranded RNA molecule. The coat protein subunits form a lattice with the triangulation number T = 3. The coat protein has a fold which is different from the fold of all other viral coat proteins so far known. It consists of a five-stranded beta sheet facing the inside of the particle, and a hairpin and two helices on the outside. The crystal structure has been refined at 2.8 A resolution. The final R-factor was 0.189 for reflections with F > 2 sigma, and the root-mean-square deviation from idealized bond lengths and bond angles was 0.015 A and 2.9 degrees, respectively. The three chemically identical conformers A, B and C are largely similar. The B conformer has a unique conformation in one loop, which is involved in 5-fold interactions, while the A and C conformers, which are involved in the quasi-6-fold contacts, are similar throughout the structure. One cis-proline has been identified in the B conformer but the corresponding prolines in A and C are of the trans isomer. This residue is conserved within small RNA coliphages and it is proposed that this isomerization enables a less elongated loop (FG) around the 5-fold axis, thus creating a channel. The extensive dimer contact supports the idea of dimers as initial building blocks. An assembly pathway is proposed where five dimers converge into a pentamer and 12 pentamers are linked together with free dimers creating a complete particle.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0022-2836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
234
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
620-39
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8254664-Amino Acid Sequence,
pubmed-meshheading:8254664-Capsid,
pubmed-meshheading:8254664-Hydrogen Bonding,
pubmed-meshheading:8254664-Levivirus,
pubmed-meshheading:8254664-Macromolecular Substances,
pubmed-meshheading:8254664-Models, Molecular,
pubmed-meshheading:8254664-Models, Structural,
pubmed-meshheading:8254664-Molecular Sequence Data,
pubmed-meshheading:8254664-Protein Conformation,
pubmed-meshheading:8254664-Protein Structure, Secondary,
pubmed-meshheading:8254664-RNA Viruses,
pubmed-meshheading:8254664-Sequence Homology, Amino Acid,
pubmed-meshheading:8254664-X-Ray Diffraction
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pubmed:year |
1993
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pubmed:articleTitle |
The refined structure of bacteriophage MS2 at 2.8 A resolution.
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pubmed:affiliation |
Department of Molecular Biology, Uppsala University Uppsala Biomedical Centre, Sweden.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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