Complementing structural information of modular proteins with small angle neutron scattering and contrast variation
| Autor: | 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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| Rok vydání: | 2007 |
| Předmět: |
Models
Molecular Conformational change Saccharomyces cerevisiae Proteins RNase P Protein subunit Neutron diffraction Biophysics Neutron scattering X-Ray Diffraction Catalytic Domain Nucleic Acids Endoribonucleases Mitochondrial Precursor Protein Import Complex Proteins Scattering Small Angle Escherichia coli Scattering Chemistry Membrane Proteins Proteins General Medicine Small-angle neutron scattering Crystallography Neutron Diffraction RNA Macromolecule Protein Binding |
| Zdroj: | European biophysics journal : EBJ. 37(5) |
| ISSN: | 0175-7571 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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