Abstract

The dynamism of proteins is central to their function, and several proteins have beendescribed as flexible, as consisting of multiple domains joined by flexible linkers, and even asintrinsically disordered. Several techniques exist to study protein structures, but small angle X-rayscattering (SAXS) has proven to be particularly powerful for the quantitative analysis of such flexiblesystems. In the present report, we have used SAXS in combination with X-ray crystallographyto highlight their usefulness at characterizing flexible proteins, using as examples two proteinsinvolved 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, slightlyelongated 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 mutatedtarget in the Shwachman-Diamond Syndrome. In solution, this protein coexists in an ensemble ofthree main conformations, with the N- and C-terminal ends adopting different orientations withrespect to the central domain. The structure observed in the protein crystal corresponds to an average of those predicted by the SAXS flexibility analysis.

Autore Pugliese

• Altamura Davide , Siliqi Dritan

Tutti gli autori

• D. Siliqi ; J. Foadi ; M. Mazzorana; D. Altamura; A. Méndez-Godoy ; N. Sánchez-Puig

Titolo volume/Rivista

Crystals

Anno di pubblicazione

2018

ISSN

2073-4352

ISBN

Non Disponibile

Numero di citazioni Wos

Nessuna citazione

Ultimo Aggiornamento Citazioni

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Numero di citazioni Scopus

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Ultimo Aggiornamento Citazioni

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Settori ERC

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Codici ASJC

Non Disponibile