| pubmed-article:11371161 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11371161 | lifeskim:mentions | umls-concept:C0206397 | lld:lifeskim |
| pubmed-article:11371161 | lifeskim:mentions | umls-concept:C1623051 | lld:lifeskim |
| pubmed-article:11371161 | lifeskim:mentions | umls-concept:C1069851 | lld:lifeskim |
| pubmed-article:11371161 | lifeskim:mentions | umls-concept:C0085475 | lld:lifeskim |
| pubmed-article:11371161 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:11371161 | lifeskim:mentions | umls-concept:C0006933 | lld:lifeskim |
| pubmed-article:11371161 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:11371161 | pubmed:dateCreated | 2001-5-23 | lld:pubmed |
| pubmed-article:11371161 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11371161 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11371161 | pubmed:abstractText | 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. | lld:pubmed |
| pubmed-article:11371161 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11371161 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11371161 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11371161 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11371161 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11371161 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11371161 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11371161 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11371161 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11371161 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:11371161 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:11371161 | pubmed:author | pubmed-author:PerhamR NRN | lld:pubmed |
| pubmed-article:11371161 | pubmed:author | pubmed-author:PedersonD MDM | lld:pubmed |
| pubmed-article:11371161 | pubmed:author | pubmed-author:MarvinD ADA | lld:pubmed |
| pubmed-article:11371161 | pubmed:author | pubmed-author:YuMM | lld:pubmed |
| pubmed-article:11371161 | pubmed:author | pubmed-author:SampsonMM | lld:pubmed |
| pubmed-article:11371161 | pubmed:author | pubmed-author:SlaterM RMR | lld:pubmed |
| pubmed-article:11371161 | pubmed:author | pubmed-author:WelshL CLC | lld:pubmed |
| pubmed-article:11371161 | pubmed:copyrightInfo | Copyright 2001 Academic Press. | lld:pubmed |
| pubmed-article:11371161 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11371161 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:11371161 | pubmed:volume | 309 | lld:pubmed |
| pubmed-article:11371161 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11371161 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11371161 | pubmed:pagination | 401-21 | lld:pubmed |
| pubmed-article:11371161 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:11371161 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11371161 | pubmed:articleTitle | The protein capsid of filamentous bacteriophage PH75 from Thermus thermophilus. | lld:pubmed |
| pubmed-article:11371161 | pubmed:affiliation | Cambridge Centre for Molecular Recognition, Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, UK. | lld:pubmed |
| pubmed-article:11371161 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11371161 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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