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==Filamentous Bacteriophage PH75== | |||
<StructureSection load='1hgv' size='340' side='right'caption='[[1hgv]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1hgv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_phage_PH75 Thermus phage PH75]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HGV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HGV FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Fiber diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hgv OCA], [https://pdbe.org/1hgv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hgv RCSB], [https://www.ebi.ac.uk/pdbsum/1hgv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hgv ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CAPSD_BPH75 CAPSD_BPH75] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
== | |||
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. | ||
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<ref>PMID:11371161</ref> | |||
The protein capsid of filamentous bacteriophage PH75 from Thermus thermophilus., Pederson DM, Welsh LC, Marvin DA, Sampson M, Perham RN, Yu M, Slater MR | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1hgv" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermus phage PH75]] | |||
[[Category: Marvin DA]] | |||
[[Category: Pederson DM]] | |||
[[Category: Perham RN]] | |||
[[Category: Sampson M]] | |||
[[Category: Slater MR]] | |||
[[Category: Welsh LC]] | |||
[[Category: Yu M]] | |||
Latest revision as of 15:25, 13 December 2023
Filamentous Bacteriophage PH75Filamentous Bacteriophage PH75
Structural highlights
FunctionPublication Abstract from PubMedThe 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 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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