1tx9
From Proteopedia
(New page: 200px<br /><applet load="1tx9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tx9, resolution 3.31Å" /> '''gpd prior to capsid ...) |
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| - | [[Image:1tx9.gif|left|200px]]<br /><applet load="1tx9" size=" | + | [[Image:1tx9.gif|left|200px]]<br /><applet load="1tx9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tx9, resolution 3.31Å" /> | caption="1tx9, resolution 3.31Å" /> | ||
'''gpd prior to capsid assembly'''<br /> | '''gpd prior to capsid assembly'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of bacteriophage phiX174 external | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1TX9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_phix174 Enterobacteria phage phix174]. Full crystallographic information is available from [http:// | + | 1TX9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_phix174 Enterobacteria phage phix174]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TX9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Enterobacteria phage phix174]] | [[Category: Enterobacteria phage phix174]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Fane, B | + | [[Category: Fane, B A.]] |
[[Category: Fisher, M.]] | [[Category: Fisher, M.]] | ||
[[Category: Kanamaru, K.]] | [[Category: Kanamaru, K.]] | ||
| - | [[Category: Morais, M | + | [[Category: Morais, M C.]] |
| - | [[Category: Rossmann, M | + | [[Category: Rossmann, M G.]] |
[[Category: assembly]] | [[Category: assembly]] | ||
[[Category: conformational switching]] | [[Category: conformational switching]] | ||
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[[Category: scaffolding protein]] | [[Category: scaffolding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:18:21 2008'' |
Revision as of 13:18, 21 February 2008
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gpd prior to capsid assembly
Overview
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.
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
Page seeded by OCA on Thu Feb 21 15:18:21 2008
