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3c5b

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[[Image:3c5b.jpg|left|200px]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3c5b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c5b OCA], [http://www.ebi.ac.uk/pdbsum/3c5b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3c5b RCSB]</span>
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'''De Novo Model of Bacteriophage Epsilon 15 Major Capsid Protein GP7'''
'''De Novo Model of Bacteriophage Epsilon 15 Major Capsid Protein GP7'''
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[[Category: King, J.]]
[[Category: King, J.]]
[[Category: Weigele, P R.]]
[[Category: Weigele, P R.]]
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[[Category: capsid protein]]
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[[Category: Capsid protein]]
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[[Category: hk97 fold]]
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[[Category: Hk97 fold]]
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[[Category: icosahedral virus]]
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[[Category: Icosahedral virus]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 21:21:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:30:41 2008''
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Revision as of 18:21, 4 May 2008

Template:STRUCTURE 3c5b

De Novo Model of Bacteriophage Epsilon 15 Major Capsid Protein GP7


Overview

A half-century after the determination of the first three-dimensional crystal structure of a protein, more than 40,000 structures ranging from single polypeptides to large assemblies have been reported. The challenge for crystallographers, however, remains the growing of a diffracting crystal. Here we report the 4.5-A resolution structure of a 22-MDa macromolecular assembly, the capsid of the infectious epsilon15 (epsilon15) particle, by single-particle electron cryomicroscopy. From this density map we constructed a complete backbone trace of its major capsid protein, gene product 7 (gp7). The structure reveals a similar protein architecture to that of other tailed double-stranded DNA viruses, even in the absence of detectable sequence similarity. However, the connectivity of the secondary structure elements (topology) in gp7 is unique. Protruding densities are observed around the two-fold axes that cannot be accounted for by gp7. A subsequent proteomic analysis of the whole virus identifies these densities as gp10, a 12-kDa protein. Its structure, location and high binding affinity to the capsid indicate that the gp10 dimer functions as a molecular staple between neighbouring capsomeres to ensure the particle's stability. Beyond epsilon15, this method potentially offers a new approach for modelling the backbone conformations of the protein subunits in other macromolecular assemblies at near-native solution states.

About this Structure

3C5B is a Single protein structure of sequence from Enterobacteria phage epsilon15. Full crystallographic information is available from OCA.

Reference

Backbone structure of the infectious epsilon15 virus capsid revealed by electron cryomicroscopy., Jiang W, Baker ML, Jakana J, Weigele PR, King J, Chiu W, Nature. 2008 Feb 28;451(7182):1130-4. PMID:18305544 Page seeded by OCA on Sun May 4 21:21:48 2008

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