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Structural Biology Unit

Laboratory 5

Biological complexity is often associated with processes which require highly accurate and regulated protein interactions. Examples of such complexity can be found in the assembly pathway of viruses or in the molecular mechanism of "gene expression". Our research aims to understand how large multi-component proteins assemble, function and interact in the cellular context.

One line of investigation is directed to the understanding of virus structures and Evolution, their assembly principles and to the virus-cell recognition mechanisms. Indeed, viruses represent a source of wonder as miniaturized entities that permeate and cross-interact with the entire biosphere and are by far the most numerous organisms on earth. Some of them are, however, pathogens and represent a threat to human and animal health. The understanding of virus morphogenesis and virus-host recognition mechanisms is fundamental in the development of antiviral drugs.

The second line of research is focused on the elucidation of transcription initiation and regulation using Archaea as a model system for Eukarya. 

Research in our group is focused on the structural analysis by cryo-electron microscopy (using our in-house JEOL JEM-2200FS Field Emission TEM with a digital camera and a in-column energy Omega Filter) and crystallography techniques of non-infectious viral particles and of the archaeal RNA polymerase transcription machinery.

COLLABORATIONS

• Prof. D. H. Bamford & Dr. H. Oksanen (Finnish Centre of Excellence in Virus Research, University of Helsinki, Finland).
• Prof. S. D. Bell (Molecular and Cellular Biochemistry Dept., Indiana University, USA).
• Prof. D. I. Stuart (WTCHG-University of Oxford, UK).
  

Principal Investigator

Laboratory members

Publications

Wojtas, M.N. and Abrescia, N.G.A.; Archaeal transcription: making up for lost time. Biochem. Soc. Trans. 41, 357-61 (2013)

Abrescia N.G.A., Bamford D.H., Grimes J.M., Stuart D.I.; Structure Unifies the viral universe. Ann. Rev. Biochem. 81, (2012)

Badia-Martinez D., Peralta B., Andres G., Guerra M., Gil-Carton D., Abrescia N.G.A.; Three-dimensional visualization of forming Hepatitis C virus-like particles by electron-tomography. Virology 430, 120-126 (2012)

Wojtas M.N., Mogni M., Millet O., Bell S.D. and Abrescia N.G.A. ; Structural and functional analyses of the interaction of archaeal RNA polymerase with DNA. Nucleic Acids Res. doi: 10.1093/nar/gks692 (2012)

Wojtas, M.N. & Abrescia, N.G.A ; Soaking DNA into crystals of archaeal RNA polymerase achieved by desalting in droplets . Acta Crystallogr. F68, 1134-8 (2012)

Abrescia, N.G.A.; Algunos de los retos pasados y futuros de la Virologia Estructural. Virologia (Publicacion Oficial de la Sociedad Espanola de Virologia) 15, 16 (2012)

Abrescia N.G.A, Grimes J.M, Oksanen H.M., Bamford J.K.H, Bamford D.H. & Stuart D.I.; The use of low resolution phasing followed by phase extension from 7.6Å to 2.5Å resolution with non-crystallographic symmetry to solve the structure of a bacteriophage capsid protein. Acta Cryst. D67, 228-232 (2011)

Wojtas M., Peralta B., Ondiviela M., Mogni M., Bell S.D and Abrescia N.G.A.; Archaeal RNA polymerase: the influence of the protruding stalk in crystal packing and preliminary biophysical analysis of the Rpo13 subunit. Biochem. Soc. Trans. 39, 25-30 (2011)

El Omari, Dhaliwal, B., Ren, J., Abrescia, N. G. A., Lockyer, M., Powell, K. L., Hawkins, A. R., Stammers, D. K. ; Structures of respiratory syncytial virus nucleocapsid protein from two crystal forms: details of potential packing interactions in the native helical form. . Acta Crystallogr F67, 1179-83. (2011)

Abrescia N. G. A., Grimes J. M., Fry E. E., Ravantti J. J., Bamford D. H. and Stuart D. I.; What Does it Take to Make a Virus: The Concept of the Viral ‘Self’. In: Stockley, P. and Twarock, R., Emerging Topics in Physical Virology (London: Imperial College Press) (2010)

Korkhin Y., Unligil, U. M., Littlefield, O., Nelson, P. J., Stuart, D. I., Sigler, P. B., Bell, S. D. and Abrescia, N. G. A.; Evolution of Complex RNA Polymerases: the Complete Archaeal RNA Polymerase Structure. Plos Biology 7, 5 e1000102. doi:10.1371/journal.pbio.1000102 (2009)

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