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| - | [[Image:1ql2.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1ql2| PDB=1ql2 | SCENE= }} | | {{STRUCTURE_1ql2| PDB=1ql2 | SCENE= }} |
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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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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_10666593}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10666593 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10666593}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Inovirus]] | | [[Category: Inovirus]] |
| | [[Category: Ssdna viruse]] | | [[Category: Ssdna viruse]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:24:11 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:17:11 2008'' |
Revision as of 10:17, 27 July 2008
Template:STRUCTURE 1ql2
INOVIRUS (FILAMENTOUS BACTERIOPHAGE) STRAIN PF1 MAJOR COAT PROTEIN ASSEMBLY
Template:ABSTRACT PUBMED 10666593
About this Structure
1QL2 is a Single protein structure of sequence from Pseudomonas phage pf1. Full crystallographic information is available from OCA.
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:10666593
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