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| [[Image:1tx9.gif|left|200px]] | | {{Seed}} |
| | [[Image:1tx9.png|left|200px]] |
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| {{STRUCTURE_1tx9| PDB=1tx9 | SCENE= }} | | {{STRUCTURE_1tx9| PDB=1tx9 | SCENE= }} |
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| '''gpd prior to capsid assembly'''
| | ===gpd prior to capsid assembly=== |
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| ==Overview==
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| The three-dimensional structure of bacteriophage phiX174 external scaffolding protein D, prior to its interaction with other structural proteins, has been determined to 3.3 angstroms by X-ray crystallography. The crystals belong to space group P4(1)2(1)2 with a dimer in the asymmetric unit that closely resembles asymmetric dimers observed in the phiX174 procapsid structure. Furthermore, application of the crystallographic 4(1) symmetry operation to one of these dimers generates a tetramer similar to the tetramer in the icosahedral asymmetric unit of the procapsid. These data suggest that both dimers and tetramers of the D protein are true morphogenetic intermediates and can form independently of other proteins involved in procapsid morphogenesis. The crystal structure of the D scaffolding protein thus represents the state of the polypeptide prior to procapsid assembly. Hence, comparison with the procapsid structure provides a rare opportunity to follow the conformational switching events necessary for the construction of complex macromolecular assemblies. | | The line below this paragraph, {{ABSTRACT_PUBMED_15383287}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15383287 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15383287}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Phix174]] | | [[Category: Phix174]] |
| [[Category: Scaffolding protein]] | | [[Category: Scaffolding protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:28:50 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:50:53 2008'' |
