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Science 29 July 1994:
Vol. 265. no. 5172, pp. 671 - 674
DOI: 10.1126/science.8036516
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Articles

Science, Vol 265, Issue 5172, 671-674
Copyright © 1994 by American Association for the Advancement of Science

articles

Pf1 virus structure: helical coat protein and DNA with paraxial phosphates

DJ Liu and LA Day

Public Health Research Institute, New York, NY 10016.

The helical path of the DNA in filamentous bacteriophage Pf1 was deduced from different kinds of existing structural information, including results from x-ray fiber diffraction. The DNA has the same pitch, 16 angstroms, as the surrounding helix of protein subunits; the rise and rotation per nucleotides are 6.1 angstroms and 132 degrees, respectively; and the phosphates are 2.5 angstroms from the axis. The DNA in Pf1 is, therefore, the most extended and twisted DNA structure known. On the basis of the DNA structure and extensive additional information about the protein, a model of the virion is proposed. In the model, the DNA bases reach out, into the protein, and the lysine and arginine side chains reach in, between the DNA bases, to stabilize the paraxial phosphate charges; the conformation of the protein subunit is a combination of alpha and 3(10) helices.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Conformational dynamics of an intact virus: Order parameters for the coat protein of Pf1 bacteriophage.
J. L. Lorieau, L. A. Day, and A. E. McDermott (2008)
PNAS 105, 10366-10371
   Abstract »    Full Text »    PDF »
Bacteriophage and Phenotypic Variation in Pseudomonas aeruginosa Biofilm Development.
J. S. Webb, M. Lau, and S. Kjelleberg (2004)
J. Bacteriol. 186, 8066-8073
   Abstract »    Full Text »    PDF »
The rise of single-molecule DNA biochemistry.
A. Rich (1998)
PNAS 95, 13999-14000
   Full Text »    PDF »
Stretched and overwound DNA forms a Pauling-like structure with exposed bases.
J. F. Allemand, D. Bensimon, R. Lavery, and V. Croquette (1998)
PNAS 95, 14152-14157
   Abstract »    Full Text »    PDF »


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