Structural and functional similarities between the capsid proteins of bacteriophages T4 and HK97 point to a common ancestry
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- Andrei Fokine
- Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, IN 47907; Laboratory of Molecular Bioengineering, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, 16/10 Miklukho-Maklaya Street, 117997 Moscow, Russia; X-Ray Crystallography Facility/Office of Science and Technology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, Building 50, Room 1345, 50 South Drive, MSC 8023, Bethesda, MD 20892; Laboratory of Structural Biology, National...
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- Petr G. Leiman
- Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, IN 47907; Laboratory of Molecular Bioengineering, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, 16/10 Miklukho-Maklaya Street, 117997 Moscow, Russia; X-Ray Crystallography Facility/Office of Science and Technology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, Building 50, Room 1345, 50 South Drive, MSC 8023, Bethesda, MD 20892; Laboratory of Structural Biology, National...
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- Mikhail M. Shneider
- Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, IN 47907; Laboratory of Molecular Bioengineering, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, 16/10 Miklukho-Maklaya Street, 117997 Moscow, Russia; X-Ray Crystallography Facility/Office of Science and Technology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, Building 50, Room 1345, 50 South Drive, MSC 8023, Bethesda, MD 20892; Laboratory of Structural Biology, National...
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- Bijan Ahvazi
- Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, IN 47907; Laboratory of Molecular Bioengineering, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, 16/10 Miklukho-Maklaya Street, 117997 Moscow, Russia; X-Ray Crystallography Facility/Office of Science and Technology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, Building 50, Room 1345, 50 South Drive, MSC 8023, Bethesda, MD 20892; Laboratory of Structural Biology, National...
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- Karen M. Boeshans
- Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, IN 47907; Laboratory of Molecular Bioengineering, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, 16/10 Miklukho-Maklaya Street, 117997 Moscow, Russia; X-Ray Crystallography Facility/Office of Science and Technology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, Building 50, Room 1345, 50 South Drive, MSC 8023, Bethesda, MD 20892; Laboratory of Structural Biology, National...
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- Alasdair C. Steven
- Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, IN 47907; Laboratory of Molecular Bioengineering, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, 16/10 Miklukho-Maklaya Street, 117997 Moscow, Russia; X-Ray Crystallography Facility/Office of Science and Technology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, Building 50, Room 1345, 50 South Drive, MSC 8023, Bethesda, MD 20892; Laboratory of Structural Biology, National...
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- Lindsay W. Black
- Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, IN 47907; Laboratory of Molecular Bioengineering, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, 16/10 Miklukho-Maklaya Street, 117997 Moscow, Russia; X-Ray Crystallography Facility/Office of Science and Technology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, Building 50, Room 1345, 50 South Drive, MSC 8023, Bethesda, MD 20892; Laboratory of Structural Biology, National...
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- Vadim V. Mesyanzhinov
- Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, IN 47907; Laboratory of Molecular Bioengineering, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, 16/10 Miklukho-Maklaya Street, 117997 Moscow, Russia; X-Ray Crystallography Facility/Office of Science and Technology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, Building 50, Room 1345, 50 South Drive, MSC 8023, Bethesda, MD 20892; Laboratory of Structural Biology, National...
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- Michael G. Rossmann
- Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, IN 47907; Laboratory of Molecular Bioengineering, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, 16/10 Miklukho-Maklaya Street, 117997 Moscow, Russia; X-Ray Crystallography Facility/Office of Science and Technology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, Building 50, Room 1345, 50 South Drive, MSC 8023, Bethesda, MD 20892; Laboratory of Structural Biology, National...
書誌事項
- 公開日
- 2005-05-06
- DOI
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- 10.1073/pnas.0502164102
- 公開者
- Proceedings of the National Academy of Sciences
この論文をさがす
説明
<jats:p> Gene product (gp) 24 of bacteriophage T4 forms the pentameric vertices of the capsid. Using x-ray crystallography, we found the principal domain of gp24 to have a polypeptide fold similar to that of the HK97 phage capsid protein plus an additional insertion domain. Fitting gp24 monomers into a cryo-EM density map of the mature T4 capsid suggests that the insertion domain interacts with a neighboring subunit, effecting a stabilization analogous to the covalent crosslinking in the HK97 capsid. Sequence alignment and genetic data show that the folds of gp24 and the hexamer-forming capsid protein, gp23 <jats:sup>*</jats:sup> , are similar. Accordingly, models of gp24 <jats:sup>*</jats:sup> pentamers, gp23 <jats:sup>*</jats:sup> hexamers, and the whole capsid were built, based on a cryo-EM image reconstruction of the capsid. Mutations in gene 23 that affect capsid shape map to the capsomer's periphery, whereas mutations that allow gp23 to substitute for gp24 at the vertices modify the interactions between monomers within capsomers. Structural data show that capsid proteins of most tailed phages, and some eukaryotic viruses, may have evolved from a common ancestor. </jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 102 (20), 7163-7168, 2005-05-06
Proceedings of the National Academy of Sciences
