1ql2: Difference between revisions
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'''INOVIRUS (FILAMENTOUS BACTERIOPHAGE) STRAIN PF1 MAJOR COAT PROTEIN ASSEMBLY''' | '''INOVIRUS (FILAMENTOUS BACTERIOPHAGE) STRAIN PF1 MAJOR COAT PROTEIN ASSEMBLY''' | ||
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[[Category: Symmons, M F.]] | [[Category: Symmons, M F.]] | ||
[[Category: Welsh, L C.]] | [[Category: Welsh, L C.]] | ||
[[Category: | [[Category: Helical virus]] | ||
[[Category: | [[Category: Helical virus coat protein]] | ||
[[Category: | [[Category: Inovirus]] | ||
[[Category: | [[Category: Ssdna viruse]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:24:11 2008'' | |||
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Revision as of 06:24, 3 May 2008
INOVIRUS (FILAMENTOUS BACTERIOPHAGE) STRAIN PF1 MAJOR COAT PROTEIN ASSEMBLY
OverviewOverview
The major coat protein in the capsid of Pf1 filamentous bacteriophage (Inovirus) forms a helical assembly of about 7000 identical protein subunits, each of which contains 46 amino-acid residues and can be closely approximated by a single gently curved alpha-helix. Since the viral DNA occupies the core of the tubular capsid and appears to make no significant specific interactions with the capsid proteins, the capsid is a simple model system for the study of the static and dynamic properties of alpha-helix assembly. The capsid undergoes a reversible temperature-induced structural transition at about 283 K between two slightly different helix forms. The two forms can coexist without an intermediate state, consistent with a first-order structural phase transition. The molecular model of the higher temperature form was refined using improved X-ray fibre diffraction data and new refinement and validation methods. The refinement indicates that the two forms are related by a change in the orientation of the capsid subunits within the virion, without a significant change in local conformation of the subunits. On the higher temperature diffraction pattern there is a region of observed intensity that is not consistent with a simple helix of identical subunits; it is proposed that the structure involves groups of three subunits which each have a slightly different orientation within the group. The grouping of subunits suggests that a change in subunit libration frequency could be the basis of the Pf1 structural transition; calculations from the model are used to explore this idea.
About this StructureAbout this Structure
1QL2 is a Single protein structure of sequence from Pseudomonas phage pf1. Full crystallographic information is available from OCA.
ReferenceReference
The molecular structure and structural transition of the alpha-helical capsid in filamentous bacteriophage Pf1., Welsh LC, Symmons MF, Marvin DA, Acta Crystallogr D Biol Crystallogr. 2000 Feb;56(Pt 2):137-50. PMID:10666593 Page seeded by OCA on Sat May 3 06:24:11 2008