1ql1: Difference between revisions
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[[Image:1ql1.gif|left|200px]] | [[Image:1ql1.gif|left|200px]] | ||
'''INOVIRUS (FILAMENTOUS BACTERIOPHAGE) STRAIN PF1 MAJOR COAT PROTEIN ASSEMBLY''' | {{Structure | ||
|PDB= 1ql1 |SIZE=350|CAPTION= <scene name='initialview01'>1ql1</scene>, resolution 3.1Å | |||
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|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
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'''INOVIRUS (FILAMENTOUS BACTERIOPHAGE) STRAIN PF1 MAJOR COAT PROTEIN ASSEMBLY''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1QL1 is a [ | 1QL1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_phage_pf1 Pseudomonas phage pf1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QL1 OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10666593 10666593] | ||
[[Category: Pseudomonas phage pf1]] | [[Category: Pseudomonas phage pf1]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: helical virus coat protein]] | [[Category: helical virus coat protein]] | ||
[[Category: inovirus]] | [[Category: inovirus]] | ||
[[Category: ssdna | [[Category: ssdna viruse]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:39:04 2008'' | ||
Revision as of 14:39, 20 March 2008
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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
1QL1 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
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