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1tx9
From Proteopedia
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| - | [[Image:1tx9.gif|left|200px]] | + | [[Image:1tx9.gif|left|200px]] |
| - | + | ||
| - | '''gpd prior to capsid assembly''' | + | {{Structure |
| + | |PDB= 1tx9 |SIZE=350|CAPTION= <scene name='initialview01'>1tx9</scene>, resolution 3.31Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= D ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10847 Enterobacteria phage phiX174]) | ||
| + | }} | ||
| + | |||
| + | '''gpd prior to capsid assembly''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TX9 is a [ | + | 1TX9 is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15383287 15383287] |
[[Category: Enterobacteria phage phix174]] | [[Category: Enterobacteria phage phix174]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: scaffolding protein]] | [[Category: scaffolding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:24:23 2008'' |
Revision as of 12:24, 20 March 2008
| |||||||
| , resolution 3.31Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | D (Enterobacteria phage phiX174) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mar 20 14:24:23 2008
