Complementing structural information of modular proteins with small angle neutron scattering and contrast variation |
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Authors: | J G Grossmann A J Callaghan M J Marcaida B F Luisi F H Alcock K Tokatlidis M Moulin M Haertlein P Timmins |
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Institution: | Molecular Biophysics Group, STFC Daresbury Laboratory, Daresbury Science and Innovation Campus, Warrington, Cheshire WA4 AD, UK. j.g.grossmann@dl.ac.uk |
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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. |
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Keywords: | Small angle neutron scattering Contrast variation X-ray scattering RNase E Allosteric mechanism TIM10 |
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