Autor:	F. Zemlin, E. Beckmann, Rudi Lurz, Elena V. Orlova, Prakash Dube, Thomas A. Trautner, Paulo Tavares, Marin van Heel
Rok vydání:	1999
Předmět:	Tentacle Bacteriophage SPP1 Mutant Fold (geology) Conical surface Biology Biochemistry Oligomer law.invention chemistry.chemical_compound Crystallography chemistry Structural Biology law Genetics Electron microscope DNA
Zdroj:	Nature Structural Biology. 6:842-846
ISSN:	1072-8368
Popis:	We have determined the three-dimensional structure of bacteriophage SPP1 portal protein (gp6) using electron microscopy at liquid-helium temperatures and angular reconstitution. The 13-fold symmetric gp6 oligomer is a turbine-shaped structure with three distinct regions: a conical stem with a central channel; the turbine wings region; and a fringe of small 'tentacles' at the end of the channel exposed to the viral head interior. The tentacle region appears flexible and may be associated with a particular function — sensing when the correct amount of DNA has been packaged. The three-dimensional structure of the gp6 SizA mutant, which packages a smaller chromosome, reveals significant differences in that region.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::c947b79af2783da2df38606ada07e75a https://doi.org/10.1038/12303 Zobrazit plný text záznamu Full text from SpringerLink