Bacteriophage T5 Structure Reveals Similarities with HK97 and T4 Suggesting Evolutionary Relationships

Bacteriophage T5 Structure Reveals Similarities with HK97 and T4 Suggesting Evolutionary... Evolutionary relationships between viruses may be obscure by protein sequence but unmasked by structure. Analysis of bacteriophage T5 by cryo-electron microscopy and protein sequence analysis reveals analogies with HK97 and T4 that suggest a mosaic of such connections. The T5 capsid is consistent with the HK97 capsid protein fold but has a different geometry, incorporating three additional hexamers on each icosahedral facet. Similarly to HK97, the T5 major capsid protein has an N-terminal extension, or Δ-domain that is missing in the mature capsid, and by analogy with HK97, may function as an assembly or scaffold domain. This Δ-domain is predicted to be largely coiled-coil, as for that of HK97, but is ∼70% longer correlating with the larger capsid. Thus, capsid architecture appears likely to be specified by the Δ-domain. Unlike HK97, the T5 capsid binds a decoration protein in the center of each hexamer similarly to the “hoc” protein of phage T4, suggesting a common role for these molecules. The tail-tube has unusual trimeric symmetry that may aid in the unique two-stage DNA-ejection process, and joins the tail-tip at a disk where tail fibers attach. This intriguing mix of characteristics embodied by phage T5 offers insights into virus assembly, subunit function, and the evolutionary connections between related viruses. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Molecular Biology Elsevier

Bacteriophage T5 Structure Reveals Similarities with HK97 and T4 Suggesting Evolutionary Relationships

Loading next page...
 
/lp/elsevier/bacteriophage-t5-structure-reveals-similarities-with-hk97-and-t4-K0olKdGa6k
Publisher
Elsevier
Copyright
Copyright © 2006 Elsevier Ltd
ISSN
0022-2836
D.O.I.
10.1016/j.jmb.2006.06.081
Publisher site
See Article on Publisher Site

Abstract

Evolutionary relationships between viruses may be obscure by protein sequence but unmasked by structure. Analysis of bacteriophage T5 by cryo-electron microscopy and protein sequence analysis reveals analogies with HK97 and T4 that suggest a mosaic of such connections. The T5 capsid is consistent with the HK97 capsid protein fold but has a different geometry, incorporating three additional hexamers on each icosahedral facet. Similarly to HK97, the T5 major capsid protein has an N-terminal extension, or Δ-domain that is missing in the mature capsid, and by analogy with HK97, may function as an assembly or scaffold domain. This Δ-domain is predicted to be largely coiled-coil, as for that of HK97, but is ∼70% longer correlating with the larger capsid. Thus, capsid architecture appears likely to be specified by the Δ-domain. Unlike HK97, the T5 capsid binds a decoration protein in the center of each hexamer similarly to the “hoc” protein of phage T4, suggesting a common role for these molecules. The tail-tube has unusual trimeric symmetry that may aid in the unique two-stage DNA-ejection process, and joins the tail-tip at a disk where tail fibers attach. This intriguing mix of characteristics embodied by phage T5 offers insights into virus assembly, subunit function, and the evolutionary connections between related viruses.

Journal

Journal of Molecular BiologyElsevier

Published: Sep 1, 2006

References

  • The bacteriophages
    McCorquodale, D.J.; Warner, H.R.
  • Protein-mediated DNA transfer into liposomes
    Lambert, O.; Plancon, L.; Rigaud, J.L.; Letellier, L.
  • Bacteriophage HK97 head assembly
    Duda, R.L.; Martincic, K.; Xie, Z.; Hendrix, R.W.
  • Proteolytic and conformational control of virus capsid maturation: the bacteriophage HK97 system
    Conway, J.F.; Duda, R.L.; Cheng, N.; Hendrix, R.W.; Steven, A.C.
  • Combining electron microscopic with x-ray crystallographic structures
    Rossmann, M.G.; Bernal, R.; Pletnev, S.V.
  • Virus maturation: dynamics and mechanism of a stabilizing structural transition that leads to infectivity
    Steven, A.C.; Heymann, J.B.; Cheng, N.; Trus, B.L.; Conway, J.F.
  • Three-dimensional reconstruction of icosahedral particles–the uncommon line
    Fuller, S.D.; Butcher, S.J.; Cheng, R.H.; Baker, T.S.
  • A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy
    Baker, T.S.; Cheng, R.H.
  • The correlation averaging of a regularly arranged bacterial cell envelope protein
    Saxton, W.O.; Baumeister, W.
  • Multi-resolution contour-based fitting of macromolecular structures
    Chacon, P.; Wriggers, W.

You’re reading a free preview. Subscribe to read the entire article.


DeepDyve is your
personal research library

It’s your single place to instantly
discover and read the research
that matters to you.

Enjoy affordable access to
over 18 million articles from more than
15,000 peer-reviewed journals.

All for just $49/month

Explore the DeepDyve Library

Search

Query the DeepDyve database, plus search all of PubMed and Google Scholar seamlessly

Organize

Save any article or search result from DeepDyve, PubMed, and Google Scholar... all in one place.

Access

Get unlimited, online access to over 18 million full-text articles from more than 15,000 scientific journals.

Your journals are on DeepDyve

Read from thousands of the leading scholarly journals from SpringerNature, Elsevier, Wiley-Blackwell, Oxford University Press and more.

All the latest content is available, no embargo periods.

See the journals in your area

DeepDyve

Freelancer

DeepDyve

Pro

Price

FREE

$49/month
$360/year

Save searches from
Google Scholar,
PubMed

Create lists to
organize your research

Export lists, citations

Read DeepDyve articles

Abstract access only

Unlimited access to over
18 million full-text articles

Print

20 pages / month

PDF Discount

20% off