Grossmann, J.G., Callaghan, A.J., Marcaida, M.J., Luisi, B.F., Alcock, F.H. and Tokatlidis, K. (2008) Complementing structural information of modular proteins with small angle neutron scattering and contrast variation. European Biophysics Journal with Biophysics Letters, 37(5), pp. 603-611. (doi: 10.1007/s00249-008-0278-z)
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Abstract
Many macromolecules in the cell function by forming multi-component assemblies. We have applied the technique of small angle neutron scattering to study a nucleic acid–protein complex and a multi-protein complex. The results illustrate the versatility and applicability of the method to study macromolecular assemblies. The neutron scattering experiments, complementing X-ray solution scattering data, reveal that the conserved catalytic domain of RNase E, an essential ribonuclease in Escherichia coli (E. coli), undergoes a marked conformational change upon binding a 5′monophosphate–RNA substrate analogue. This provides the first evidence in support of an allosteric mechanism that brings about RNA substrate cleavage. Neutron contrast variation of the multi-protein TIM10 complex, a mitochondrial chaperone assembly comprising the subunits Tim9 and Tim10, has been used to determine a low-resolution shape reconstruction of the complex, highlighting the integral subunit organization. It shows characteristic features involving protrusions that could be assigned to the six subunits forming the complex.
Item Type: | Articles |
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Status: | Published |
Refereed: | Yes |
Glasgow Author(s) Enlighten ID: | Tokatlidis, Professor Kostas |
Authors: | Grossmann, J.G., Callaghan, A.J., Marcaida, M.J., Luisi, B.F., Alcock, F.H., and Tokatlidis, K. |
College/School: | College of Medical Veterinary and Life Sciences > School of Molecular Biosciences |
Journal Name: | European Biophysics Journal with Biophysics Letters |
Publisher: | Springer-Verlag |
ISSN: | 0175-7571 |
ISSN (Online): | 1432-1017 |
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