1tx9

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(New page: 200px<br /><applet load="1tx9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tx9, resolution 3.31&Aring;" /> '''gpd prior to capsid ...)
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[[Image:1tx9.gif|left|200px]]<br /><applet load="1tx9" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1tx9.gif|left|200px]]<br /><applet load="1tx9" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1tx9, resolution 3.31&Aring;" />
caption="1tx9, resolution 3.31&Aring;" />
'''gpd prior to capsid assembly'''<br />
'''gpd prior to capsid assembly'''<br />
==Overview==
==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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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TX9 OCA].
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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]]
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[[Category: Fane, B.A.]]
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[[Category: Fane, B A.]]
[[Category: Fisher, M.]]
[[Category: Fisher, M.]]
[[Category: Kanamaru, K.]]
[[Category: Kanamaru, K.]]
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[[Category: Morais, M.C.]]
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[[Category: Morais, M C.]]
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[[Category: Rossmann, M.G.]]
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[[Category: Rossmann, M G.]]
[[Category: assembly]]
[[Category: assembly]]
[[Category: conformational switching]]
[[Category: conformational switching]]
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[[Category: scaffolding protein]]
[[Category: scaffolding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:39:52 2007''
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''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


1tx9, resolution 3.31Å

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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

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