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The portal protein of bacteriophage SPP1: a DNA pump with 13-fold symmetry.

1993; Springer Nature; Volume: 12; Issue: 4 Linguagem: Inglês

10.1002/j.1460-2075.1993.tb05775.x

1460-2075

Priyanka Dubé, Paulo Tavares, R. Lurz, Marin van Heel,

Enzyme Structure and Function

Research Article1 April 1993free access The portal protein of bacteriophage SPP1: a DNA pump with 13-fold symmetry. P. Dube P. Dube Fritz Haber Institut der Max Planck Gesellschaft, Berlin, Germany. Search for more papers by this author P. Tavares P. Tavares Fritz Haber Institut der Max Planck Gesellschaft, Berlin, Germany. Search for more papers by this author R. Lurz R. Lurz Fritz Haber Institut der Max Planck Gesellschaft, Berlin, Germany. Search for more papers by this author M. van Heel M. van Heel Fritz Haber Institut der Max Planck Gesellschaft, Berlin, Germany. Search for more papers by this author P. Dube P. Dube Fritz Haber Institut der Max Planck Gesellschaft, Berlin, Germany. Search for more papers by this author P. Tavares P. Tavares Fritz Haber Institut der Max Planck Gesellschaft, Berlin, Germany. Search for more papers by this author R. Lurz R. Lurz Fritz Haber Institut der Max Planck Gesellschaft, Berlin, Germany. Search for more papers by this author M. van Heel M. van Heel Fritz Haber Institut der Max Planck Gesellschaft, Berlin, Germany. Search for more papers by this author Author Information P. Dube1, P. Tavares1, R. Lurz1 and M. Heel1 1Fritz Haber Institut der Max Planck Gesellschaft, Berlin, Germany. The EMBO Journal (1993)12:1303-1309https://doi.org/10.1002/j.1460-2075.1993.tb05775.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Electron microscopy in combination with image processing is a powerful method for obtaining structural information on non-crystallized biological macromolecules at the 10–50 A resolution level. The processing of noisy microscopical images requires advanced data processing methodologies in which one must carefully avoid the introduction of any form of bias into the data set. Using a novel multivariate statistical approach to the analysis of symmetry, we studied the structure of the bacteriophage SPP1 portal protein oligomer. This portal structure, ubiquitous in icosahedral bacteriophages which package dsDNA, is located at the site of symmetry mismatch between a 5-fold vertex of the icosahedral shell and the 6-fold symmetric (helical) tail. From previous studies such 'head-to-tail connector' structures were generally accepted to be homododecamers assembled in a 12-fold symmetric ring around a central channel. Using a new analysis methodology we have found that the phage SPP1 portal structure exhibits 13-fold cyclical symmetry: a new point group organization for oligomeric proteins. A model for the DNA packaging mechanism by 13-fold symmetric portal protein assemblies is presented which attributes a coherent functional meaning to their unusual symmetry. Previous ArticleNext Article Volume 12Issue 41 April 1993In this issue RelatedDetailsLoading ...