1hh0: Difference between revisions

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New page: left|200px<br /><applet load="1hh0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hh0, resolution 2.4Å" /> '''FILAMENTOUS BACTERIOP...
 
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[[Image:1hh0.gif|left|200px]]<br /><applet load="1hh0" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1hh0.gif|left|200px]]<br /><applet load="1hh0" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1hh0, resolution 2.4&Aring;" />
caption="1hh0, resolution 2.4&Aring;" />
'''FILAMENTOUS BACTERIOPHAGE PH75'''<br />
'''FILAMENTOUS BACTERIOPHAGE PH75'''<br />


==Overview==
==Overview==
The PH75 strain of filamentous bacteriophage (Inovirus) grows in the, thermophilic bacterium Thermus thermophilus at 70 degrees C. We have, characterized the viral DNA and determined the amino acid sequence of the, major coat protein, p8. The p8 protein is synthesized without a leader, sequence, like that of bacteriophage Pf3 but unlike that of bacteriophage, Pf1, both of which grow in the mesophile Pseudomonas aeruginosa. X-ray, diffraction patterns from ordered fibres of the PH75 virion are similar to, those from bacteriophages Pf1 and Pf3, indicating that the protein capsid, of the PH75 virion has the same helix symmetry and subunit shape, even, though the primary structures of the major coat proteins are quite, different and the virions assemble at very different temperatures. We have, used this information to build a molecular model of the PH75 protein, capsid based on that of Pf1, and refined the model by simulated annealing, using fibre diffraction data extending to 2.4 A resolution in the, meridional direction and to 3.1 A resolution in the equatorial direction., The common design may reflect a fundamental motif of alpha-helix packing, although differences exist in the DNA packaging and in the means of, insertion of the major coat protein of these filamentous bacteriophages, into the membrane of the host bacterial cell. These may reflect, differences in the assembly mechanisms of the virions.
The PH75 strain of filamentous bacteriophage (Inovirus) grows in the thermophilic bacterium Thermus thermophilus at 70 degrees C. We have characterized the viral DNA and determined the amino acid sequence of the major coat protein, p8. The p8 protein is synthesized without a leader sequence, like that of bacteriophage Pf3 but unlike that of bacteriophage Pf1, both of which grow in the mesophile Pseudomonas aeruginosa. X-ray diffraction patterns from ordered fibres of the PH75 virion are similar to those from bacteriophages Pf1 and Pf3, indicating that the protein capsid of the PH75 virion has the same helix symmetry and subunit shape, even though the primary structures of the major coat proteins are quite different and the virions assemble at very different temperatures. We have used this information to build a molecular model of the PH75 protein capsid based on that of Pf1, and refined the model by simulated annealing, using fibre diffraction data extending to 2.4 A resolution in the meridional direction and to 3.1 A resolution in the equatorial direction. The common design may reflect a fundamental motif of alpha-helix packing, although differences exist in the DNA packaging and in the means of insertion of the major coat protein of these filamentous bacteriophages into the membrane of the host bacterial cell. These may reflect differences in the assembly mechanisms of the virions.


==About this Structure==
==About this Structure==
1HH0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_phage_f237 Vibrio phage f237]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HH0 OCA].  
1HH0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_phage_f237 Vibrio phage f237]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HH0 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Vibrio phage f237]]
[[Category: Vibrio phage f237]]
[[Category: Marvin, D.A.]]
[[Category: Marvin, D A.]]
[[Category: Pederson, D.M.]]
[[Category: Pederson, D M.]]
[[Category: Perham, R.N.]]
[[Category: Perham, R N.]]
[[Category: Sampson, M.]]
[[Category: Sampson, M.]]
[[Category: Slater, M.R.]]
[[Category: Slater, M R.]]
[[Category: Welsh, L.C.]]
[[Category: Welsh, L C.]]
[[Category: Yu, M.]]
[[Category: Yu, M.]]
[[Category: filamentous bacteriophage]]
[[Category: filamentous bacteriophage]]
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[[Category: virus coat protein]]
[[Category: virus coat protein]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:01:07 2008''

Revision as of 14:01, 21 February 2008

File:1hh0.gif


1hh0, resolution 2.4Å

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FILAMENTOUS BACTERIOPHAGE PH75

OverviewOverview

The PH75 strain of filamentous bacteriophage (Inovirus) grows in the thermophilic bacterium Thermus thermophilus at 70 degrees C. We have characterized the viral DNA and determined the amino acid sequence of the major coat protein, p8. The p8 protein is synthesized without a leader sequence, like that of bacteriophage Pf3 but unlike that of bacteriophage Pf1, both of which grow in the mesophile Pseudomonas aeruginosa. X-ray diffraction patterns from ordered fibres of the PH75 virion are similar to those from bacteriophages Pf1 and Pf3, indicating that the protein capsid of the PH75 virion has the same helix symmetry and subunit shape, even though the primary structures of the major coat proteins are quite different and the virions assemble at very different temperatures. We have used this information to build a molecular model of the PH75 protein capsid based on that of Pf1, and refined the model by simulated annealing, using fibre diffraction data extending to 2.4 A resolution in the meridional direction and to 3.1 A resolution in the equatorial direction. The common design may reflect a fundamental motif of alpha-helix packing, although differences exist in the DNA packaging and in the means of insertion of the major coat protein of these filamentous bacteriophages into the membrane of the host bacterial cell. These may reflect differences in the assembly mechanisms of the virions.

About this StructureAbout this Structure

1HH0 is a Single protein structure of sequence from Vibrio phage f237. Full crystallographic information is available from OCA.

ReferenceReference

The protein capsid of filamentous bacteriophage PH75 from Thermus thermophilus., Pederson DM, Welsh LC, Marvin DA, Sampson M, Perham RN, Yu M, Slater MR, J Mol Biol. 2001 Jun 1;309(2):401-21. PMID:11371161

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