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Crystals 2018, 8(3), 109; https://doi.org/10.3390/cryst8030109

Conformational Flexibility of Proteins Involved in Ribosome Biogenesis: Investigations via Small Angle X-ray Scattering (SAXS)

1
Istituto di Cristallografia, Consiglio Nazionale delle Ricerche, Via G. Amendola 122/O, 70126 Bari, Italy
2
Department of Mathematical Sciences, University of Bath, Claverton Down, Bath BA2 7AY, UK
3
Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot OX11 0DE, UK
4
Departamento de Química de Biomacromoléculas, Instituto de Química, Universidad Nacional Autónoma de México, Ciudad de México 04150, Mexico
*
Authors to whom correspondence should be addressed.
Received: 31 January 2018 / Revised: 22 February 2018 / Accepted: 22 February 2018 / Published: 26 February 2018
(This article belongs to the Special Issue Recent Advances in Protein Crystallography)
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Abstract

The dynamism of proteins is central to their function, and several proteins have been described as flexible, as consisting of multiple domains joined by flexible linkers, and even as intrinsically disordered. Several techniques exist to study protein structures, but small angle X-ray scattering (SAXS) has proven to be particularly powerful for the quantitative analysis of such flexible systems. In the present report, we have used SAXS in combination with X-ray crystallography to highlight their usefulness at characterizing flexible proteins, using as examples two proteins involved in different steps of ribosome biogenesis. The yeast BRCA2 and CDKN1A-interactig protein, Bcp1, is a chaperone for Rpl23 of unknown structure. We showed that it consists of a rigid, slightly elongated protein, with a secondary structure comprising a mixture of alpha helices and beta sheets. As an example of a flexible molecule, we studied the SBDS (Shwachman-Bodian-Diamond Syndrome) protein that is involved in the cytoplasmic maturation of the 60S subunit and constitutes the mutated target in the Shwachman-Diamond Syndrome. In solution, this protein coexists in an ensemble of three main conformations, with the N- and C-terminal ends adopting different orientations with respect to the central domain. The structure observed in the protein crystal corresponds to an average of those predicted by the SAXS flexibility analysis. View Full-Text
Keywords: SAXS; Bcp1; SBDS; flexibility SAXS; Bcp1; SBDS; flexibility
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
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Siliqi, D.; Foadi, J.; Mazzorana, M.; Altamura, D.; Méndez-Godoy, A.; Sánchez-Puig, N. Conformational Flexibility of Proteins Involved in Ribosome Biogenesis: Investigations via Small Angle X-ray Scattering (SAXS). Crystals 2018, 8, 109.

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