Large scale analysis of protein conformational transitions from aqueous to non-aqueous media.

Abstract:

BACKGROUND:Biocatalysis in organic solvents is nowadays a common practice with a large potential in Biotechnology. Several studies report that proteins which are co-crystallized or soaked in organic solvents preserve their fold integrity showing almost identical arrangements when compared to their aqueous forms. However, it is well established that the catalytic activity of proteins in organic solvents is much lower than in water. In order to explain this diminished activity and to further characterize the behaviour of proteins in non-aqueous environments, we performed a large-scale analysis (1737 proteins) of the conformational diversity of proteins crystallized in aqueous and co-crystallized or soaked in non-aqueous media. RESULTS:Using proteins' experimentally determined conformational diversity taken from CoDNaS database, we found that proteins in non-aqueous media display much lower conformational diversity when compared to the corresponding conformers obtained in water. When conformational diversity is compared between conformers obtained in different non-aqueous media, their structural differences are larger and mostly independent of the presence of cognate ligands. We also found that conformers corresponding to non-aqueous media have larger but less flexible cavities, lower number of disordered regions and lower active-site residue mobility. CONCLUSIONS:Our results show that non-aqueous media conformers have specific structural features and that they do not adopt extreme conformations found in aqueous media. This makes them clearly different from their corresponding aqueous conformers.

journal_name

BMC Bioinformatics

journal_title

BMC bioinformatics

authors

Rueda AJV,Monzon AM,Ardanaz SM,Iglesias LE,Parisi G

doi

10.1186/s12859-018-2044-2

subject

Has Abstract

pub_date

2018-01-30 00:00:00

pages

27

issue

1

issn

1471-2105

pii

10.1186/s12859-018-2044-2

journal_volume

19

pub_type

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