1tx9: Difference between revisions

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[[Image:1tx9.gif|left|200px]]
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[[Image:1tx9.png|left|200px]]


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{{STRUCTURE_1tx9|  PDB=1tx9  |  SCENE=  }}  
{{STRUCTURE_1tx9|  PDB=1tx9  |  SCENE=  }}  


'''gpd prior to capsid assembly'''
===gpd prior to capsid assembly===




==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.
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{{ABSTRACT_PUBMED_15383287}}


==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''
 
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Revision as of 23:50, 27 July 2008

File:1tx9.png

Template:STRUCTURE 1tx9

gpd prior to capsid assembly

Template:ABSTRACT PUBMED 15383287

About this Structure

1TX9 is a Single protein structure of sequence from Enterobacteria phage phix174. Full crystallographic information is available from OCA.

Reference

Conformational switching by the scaffolding protein D directs the assembly of bacteriophage phiX174., Morais MC, Fisher M, Kanamaru S, Przybyla L, Burgner J, Fane BA, Rossmann MG, Mol Cell. 2004 Sep 24;15(6):991-7. PMID:15383287

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