Structure of the bacteriophage T4 long tail fiber receptor-binding tip
Edited by Jonathan A. King, Massachusetts Institute of Technology, Cambridge, MA, and accepted by the Editorial Board October 1, 2010 (received for review July 29, 2010)
Abstract
Bacteriophages are the most numerous organisms in the biosphere. In spite of their biological significance and the spectrum of potential applications, little high-resolution structural detail is available on their receptor-binding fibers. Here we present the crystal structure of the receptor-binding tip of the bacteriophage T4 long tail fiber, which is highly homologous to the tip of the bacteriophage lambda side tail fibers. This structure reveals an unusual elongated six-stranded antiparallel beta-strand needle domain containing seven iron ions coordinated by histidine residues arranged colinearly along the core of the biological unit. At the end of the tip, the three chains intertwine forming a broader head domain, which contains the putative receptor interaction site. The structure reveals a previously unknown beta-structured fibrous fold, provides insights into the remarkable stability of the fiber, and suggests a framework for mutations to expand or modulate receptor-binding specificity.
Data Availability
Data deposition: The coordinates and structure factors (of remote, peak, and inflection point data) have been deposited in the Protein Data Bank, www.pdb.org (PDB ID code 2XGF).
Acknowledgments.
We thank Javier Varela for N-terminal sequence analysis, Jana Alonso for mass spectroscopy, Stefan Miller for providing the gp57 expression vector and the ESRF for measurement time on beamlines BM30A, ID23-1, and ID23-2. This research was sponsored by Grant BFU2008-01588 (to M.J.v.R.), a José Castillejo fellowship (J.M.O.), and a Formacion del Profesorado Universitario Fellowship (C.G.D.) from the Spanish Ministry of Education and Science. This work was also supported by the European Commission under Contract NMP4-CT-2006-033256 and by the Xunta de Galicia via an Angeles Alvariño fellowship (J.M.O.).
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Information & Authors
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Data Availability
Data deposition: The coordinates and structure factors (of remote, peak, and inflection point data) have been deposited in the Protein Data Bank, www.pdb.org (PDB ID code 2XGF).
Submission history
Published online: November 1, 2010
Published in issue: November 23, 2010
Keywords
Acknowledgments
We thank Javier Varela for N-terminal sequence analysis, Jana Alonso for mass spectroscopy, Stefan Miller for providing the gp57 expression vector and the ESRF for measurement time on beamlines BM30A, ID23-1, and ID23-2. This research was sponsored by Grant BFU2008-01588 (to M.J.v.R.), a José Castillejo fellowship (J.M.O.), and a Formacion del Profesorado Universitario Fellowship (C.G.D.) from the Spanish Ministry of Education and Science. This work was also supported by the European Commission under Contract NMP4-CT-2006-033256 and by the Xunta de Galicia via an Angeles Alvariño fellowship (J.M.O.).
Notes
This article is a PNAS Direct Submission. J.A.K. is a guest editor invited by the Editorial Board.
Authors
Competing Interests
The authors declare no conflict of interest.
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Cite this article
Structure of the bacteriophage T4 long tail fiber receptor-binding tip, Proc. Natl. Acad. Sci. U.S.A.
107 (47) 20287-20292,
https://doi.org/10.1073/pnas.1011218107
(2010).
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