Refined structure of southern bean mosaic virus at 2.9 Å resolution
Identifieur interne : 004C86 ( Main/Exploration ); précédent : 004C85; suivant : 004C87Refined structure of southern bean mosaic virus at 2.9 Å resolution
Auteurs : Abelardo M. Silva [Argentine] ; Michael G. Rossmann [États-Unis]Source :
- Journal of Molecular Biology [ 0022-2836 ] ; 1987.
English descriptors
- Teeft :
- Amino, Atomic positions, Basic residues, Biol, Calcium ions, Capsid, Capsid assembly, Carboxyl, Carboxyl groups, Caspar klug, Coat protein, Dimer, Erickson, Harrison, Helix, Hydrogen bonds, Icosahedral, Icosahedral axes, Icosahedral axis, Icosahedral symmetry, Interface, Intersubunit contacts, Open circles, Polar interactions, Polypeptide, Polypeptide chain, Rossmann, Rossmann figure, Rotation angles, Sbmv, Shortest contacts, Silva, Silva rossmann, Southern bean mosaic virus, Southern bean mosaic virus structure, Subunit, Subunit interfaces, Superposition, Temperature factors, Type dimers, Unpublished results, Viral, Viral capsid, Virology, Water molecules.
Abstract
Abstract: The T = 3 capsid of southern bean mosaic virus is analyzed in detail. The β-sheets of the β-barrel folding motif that form the subunits show a high degree of twist, generated by several β-bulges. Only 34 water molecules were identified in association with the three quasi-equivalent subunits, most of them on the external viral surface. Subunit contacts related by quasi-3-fold axes are similar, are dominated by polar interactions and have almost identical calcium binding sites. There is no metal ion on the quasi-3-fold axis, as previously reported. Subunits related by quasi-2-fold and icosahedral 2-fold axes have different contacts but nevertheless display almost identical interactions between the antiparallel helices αA. A dipole-dipole type interaction between these helices may produce an energetically stable hinge that allows two types of dimers in a T = 3 assembly. The temperature factor distribution, the hydrogen-bonding pattern, and the contacts across the icosahedral 2-fold axes suggest that one of the dimer types is present in the intact virion and probably also in solution; the other is produced only during capsid assembly. Interactions along the 5-fold axes are mainly polar and possibly form an ion channel. The β-sheet structures of the three subunits can be superimposed with considerable precision. Significant relative distortions between quasi-equivalent subunits occur mainly in helices and loops. The two dimeric forms and the subunit distortions are the consequence of the non-equivalent subunit environments in the capsid.
Url:
DOI: 10.1016/0022-2836(87)90610-3
Affiliations:
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Silva</name><affiliation wicri:level="1"><country xml:lang="fr">Argentine</country><wicri:regionArea>Departamento de Fisica Facultad de Ciencias Exactas Universidad Nacional de La Plata C.C. No. 67, 1900 La Plata</wicri:regionArea><wicri:noRegion>1900 La Plata</wicri:noRegion></affiliation></author><author><name sortKey="Rossmann, Michael G" sort="Rossmann, Michael G" uniqKey="Rossmann M" first="Michael G." last="Rossmann">Michael G. Rossmann</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Sciences Purdue University West Lafayette, IN 47907</wicri:regionArea><wicri:noRegion>IN 47907</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Molecular Biology</title><title level="j" type="abbrev">YJMBI</title><idno type="ISSN">0022-2836</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1987">1987</date><biblScope unit="volume">197</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="69">69</biblScope><biblScope unit="page" to="87">87</biblScope></imprint><idno type="ISSN">0022-2836</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0022-2836</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Amino</term><term>Atomic positions</term><term>Basic residues</term><term>Biol</term><term>Calcium ions</term><term>Capsid</term><term>Capsid assembly</term><term>Carboxyl</term><term>Carboxyl groups</term><term>Caspar klug</term><term>Coat protein</term><term>Dimer</term><term>Erickson</term><term>Harrison</term><term>Helix</term><term>Hydrogen bonds</term><term>Icosahedral</term><term>Icosahedral axes</term><term>Icosahedral axis</term><term>Icosahedral symmetry</term><term>Interface</term><term>Intersubunit contacts</term><term>Open circles</term><term>Polar interactions</term><term>Polypeptide</term><term>Polypeptide chain</term><term>Rossmann</term><term>Rossmann figure</term><term>Rotation angles</term><term>Sbmv</term><term>Shortest contacts</term><term>Silva</term><term>Silva rossmann</term><term>Southern bean mosaic virus</term><term>Southern bean mosaic virus structure</term><term>Subunit</term><term>Subunit interfaces</term><term>Superposition</term><term>Temperature factors</term><term>Type dimers</term><term>Unpublished results</term><term>Viral</term><term>Viral capsid</term><term>Virology</term><term>Water molecules</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The T = 3 capsid of southern bean mosaic virus is analyzed in detail. The β-sheets of the β-barrel folding motif that form the subunits show a high degree of twist, generated by several β-bulges. Only 34 water molecules were identified in association with the three quasi-equivalent subunits, most of them on the external viral surface. Subunit contacts related by quasi-3-fold axes are similar, are dominated by polar interactions and have almost identical calcium binding sites. There is no metal ion on the quasi-3-fold axis, as previously reported. Subunits related by quasi-2-fold and icosahedral 2-fold axes have different contacts but nevertheless display almost identical interactions between the antiparallel helices αA. A dipole-dipole type interaction between these helices may produce an energetically stable hinge that allows two types of dimers in a T = 3 assembly. The temperature factor distribution, the hydrogen-bonding pattern, and the contacts across the icosahedral 2-fold axes suggest that one of the dimer types is present in the intact virion and probably also in solution; the other is produced only during capsid assembly. Interactions along the 5-fold axes are mainly polar and possibly form an ion channel. The β-sheet structures of the three subunits can be superimposed with considerable precision. Significant relative distortions between quasi-equivalent subunits occur mainly in helices and loops. The two dimeric forms and the subunit distortions are the consequence of the non-equivalent subunit environments in the capsid.</div></front></TEI><affiliations><list><country><li>Argentine</li><li>États-Unis</li></country></list><tree><country name="Argentine"><noRegion><name sortKey="Silva, Abelardo M" sort="Silva, Abelardo M" uniqKey="Silva A" first="Abelardo M." last="Silva">Abelardo M. Silva</name></noRegion></country><country name="États-Unis"><noRegion><name sortKey="Rossmann, Michael G" sort="Rossmann, Michael G" uniqKey="Rossmann M" first="Michael G." last="Rossmann">Michael G. Rossmann</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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