Identification of allosteric disulfides from labile bonds in X-ray structures

Identification of allosteric disulfides from labile bonds in X-ray structures.

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Item Type: Article
Status: Published
Official URL:
Journal or Publication Title: Royal Society Open Science
Volume: 5
Number: 2
Page Range: p. 171058
Date: 2018
Divisions: ACRF Centenary Cancer Research Centre
Depositing User: General Admin
Identification Number: 10.1098/rsos.171058
ISSN: 2054-5703
Date Deposited: 03 Jan 2021 22:35

Protein disulfide bonds link pairs of cysteine sulfur atoms and are either structural or functional motifs. The allosteric disulfides control the function of the protein in which they reside when cleaved or formed. Here, we identify potential allosteric disulfides in all Protein Data Bank X-ray structures from bonds that are present in some molecules of a protein crystal but absent in others, or present in some structures of a protein but absent in others. We reasoned that the labile nature of these disulfides signifies a propensity for cleavage and so possible allosteric regulation of the protein in which the bond resides. A total of 511 labile disulfide bonds were identified. The labile disulfides are more stressed than the average bond, being characterized by high average torsional strain and stretching of the sulfur-sulfur bond and neighbouring bond angles. This pre-stress likely underpins their susceptibility to cleavage. The coagulation, complement and oxygen-sensing hypoxia inducible factor-1 pathways, which are known or have been suggested to be regulated by allosteric disulfides, are enriched in proteins containing labile disulfides. The identification of labile disulfide bonds will facilitate the study of this post-translational modification.

Keywords: allosteric disulfides; coagulation; complement; oxygen-sensing; redox.

Pijning, Aster E.
Chiu, Joyce
Yeo, Reichelle X.
Wong, Jason W. H.
Hogg, Philip J.
Last Modified: 03 Jan 2021 22:35

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