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Structure of large dsDNA viruses

  • Thomas Klose

    Thomas Klose studied biochemistry at the Martin-Luther-Universität Halle-Wittenberg. He received his PhD in biochemistry from the Martin-Luther-Universität Halle-Wittenberg, where he worked within the framework of the GRK1026 on the assembly of virus-like-particles in the group of Hauke Lilie. He is currently working in the Rossmann group at Purdue University on the structure of large viruses.

     EMAIL logo     und Michael G. Rossmann

    Michael G. Rossmann was born in Frankfurt, Germany and studied physics and mathematics at the University of London. He received his PhD in chemical crystallography in 1956 from the University of Glasgow. He worked as a postdoc with William N. Lipscomb, Jr. at the University of Minnesota before returning to the UK and where he worked with Max Perutz on the structure of hemoglobin at the MRC Laboratory at the University of Cambridge. In 1964 he became a faculty member in the Department of Biological Sciences at Purdue University. He was promoted to full professor in 1967 and is the Hanley Distinguished Professor of Biological Sciences since 1978. Additionally, he has adjunct positions at Cornell University as well as Indiana University’s School of Medicine. He is an elected member of the National Academy of Sciences, a Foreign Fellow of the Indian National Science Academy and an Elected Foreign Member of the Royal Society of London. Among other honors he was awarded honorary doctorates by the University of Uppsala in Sweden, the University of Strasbourg in France, the Vrije Universiteit Brussel in Belgium, the University of Glasgow in Scotland, University of York in England and the University of Québec in Canada.
Veröffentlicht/Copyright: 8. Juli 2014
Biological Chemistry
Aus der Zeitschrift Biological Chemistry Band 395 Heft 7-8

Abstract

Nucleocytoplasmic large dsDNA viruses (NCLDVs) encompass an ever-increasing group of large eukaryotic viruses, infecting a wide variety of organisms. The set of core genes shared by all these viruses includes a major capsid protein with a double jelly-roll fold forming an icosahedral capsid, which surrounds a double layer membrane that contains the viral genome. Furthermore, some of these viruses, such as the members of the Mimiviridae and Phycodnaviridae have a unique vertex that is used during infection to transport DNA into the host.

Keywords: assembly; giant virus; nucleocytoplasmic large dsDNA virus (NCLDV); unique vertex
Corresponding author: Thomas Klose, Department of Biological Sciences, Purdue University, West Lafayette, IN 47907-2032, USA, e-mail:

About the authors

Thomas Klose

Thomas Klose studied biochemistry at the Martin-Luther-Universität Halle-Wittenberg. He received his PhD in biochemistry from the Martin-Luther-Universität Halle-Wittenberg, where he worked within the framework of the GRK1026 on the assembly of virus-like-particles in the group of Hauke Lilie. He is currently working in the Rossmann group at Purdue University on the structure of large viruses.

Michael G. Rossmann

Michael G. Rossmann was born in Frankfurt, Germany and studied physics and mathematics at the University of London. He received his PhD in chemical crystallography in 1956 from the University of Glasgow. He worked as a postdoc with William N. Lipscomb, Jr. at the University of Minnesota before returning to the UK and where he worked with Max Perutz on the structure of hemoglobin at the MRC Laboratory at the University of Cambridge. In 1964 he became a faculty member in the Department of Biological Sciences at Purdue University. He was promoted to full professor in 1967 and is the Hanley Distinguished Professor of Biological Sciences since 1978. Additionally, he has adjunct positions at Cornell University as well as Indiana University’s School of Medicine. He is an elected member of the National Academy of Sciences, a Foreign Fellow of the Indian National Science Academy and an Elected Foreign Member of the Royal Society of London. Among other honors he was awarded honorary doctorates by the University of Uppsala in Sweden, the University of Strasbourg in France, the Vrije Universiteit Brussel in Belgium, the University of Glasgow in Scotland, University of York in England and the University of Québec in Canada.

Acknowledgments

The authors are grateful for financial support from the National Institutes of Health (AI011219 to M.G.R.).

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Received: 2014-2-17
Accepted: 2014-4-23
Published Online: 2014-7-8
Published in Print: 2014-7-1

©2014 by Walter de Gruyter Berlin/Boston

Artikel in diesem Heft

  1. Frontmatter
  2. Guest Editorial
  3. Highlight: conformational transitions in macromolecular interactions
  4. Single-molecule spectroscopy of unfolded proteins and chaperonin action
  5. Influence of the polypeptide environment next to amyloidogenic peptides on fibril formation
  6. Structure of large dsDNA viruses
  7. Functional aspects of extracellular cyclophilins
  8. Generic tools for conditionally altering protein abundance and phenotypes on demand
  9. Structural insights into calmodulin/Munc13 interaction
  10. Interaction of linear polyamines with negatively charged phospholipids: the effect of polyamine charge distance
  11. Interaction of the human N-Ras protein with lipid raft model membranes of varying degrees of complexity
  12. Lanthanides as substitutes for calcium ions in the activation of plant α-type phospholipase D
  13. Insights from reconstitution reactions of COPII vesicle formation using pure components and low mechanical perturbation
  14. Identification of key residues in the formate channel FocA that control import and export of formate
  15. Twin-arginine translocation-arresting protein regions contact TatA and TatB
  16. Biophysical and biochemical analysis of hnRNP K: arginine methylation, reversible aggregation and combinatorial binding to nucleic acids
  17. An ancient oxidoreductase making differential use of its cofactors
  18. Biophysical characterization of polyomavirus minor capsid proteins
  19. Structural basis for PTPA interaction with the invariant C-terminal tail of PP2A
  20. Correlating structure and ligand affinity in drug discovery: a cautionary tale involving second shell residues
  21. Thermodynamic signatures in macromolecular interactions involving conformational flexibility
https://doi.org/10.1515/hsz-2014-0145
Schlagwörter für diesen Artikel
assembly; giant virus; nucleocytoplasmic large dsDNA virus (NCLDV); unique vertex

Artikel in diesem Heft

  1. Frontmatter
  2. Guest Editorial
  3. Highlight: conformational transitions in macromolecular interactions
  4. Single-molecule spectroscopy of unfolded proteins and chaperonin action
  5. Influence of the polypeptide environment next to amyloidogenic peptides on fibril formation
  6. Structure of large dsDNA viruses
  7. Functional aspects of extracellular cyclophilins
  8. Generic tools for conditionally altering protein abundance and phenotypes on demand
  9. Structural insights into calmodulin/Munc13 interaction
  10. Interaction of linear polyamines with negatively charged phospholipids: the effect of polyamine charge distance
  11. Interaction of the human N-Ras protein with lipid raft model membranes of varying degrees of complexity
  12. Lanthanides as substitutes for calcium ions in the activation of plant α-type phospholipase D
  13. Insights from reconstitution reactions of COPII vesicle formation using pure components and low mechanical perturbation
  14. Identification of key residues in the formate channel FocA that control import and export of formate
  15. Twin-arginine translocation-arresting protein regions contact TatA and TatB
  16. Biophysical and biochemical analysis of hnRNP K: arginine methylation, reversible aggregation and combinatorial binding to nucleic acids
  17. An ancient oxidoreductase making differential use of its cofactors
  18. Biophysical characterization of polyomavirus minor capsid proteins
  19. Structural basis for PTPA interaction with the invariant C-terminal tail of PP2A
  20. Correlating structure and ligand affinity in drug discovery: a cautionary tale involving second shell residues
  21. Thermodynamic signatures in macromolecular interactions involving conformational flexibility
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