Location of S-nitrosylated cysteines in protein three-dimensional structures

Although S-nitrosylation of cysteines is a common protein posttranslational modification, little is known about its three-dimensional structural features. This paper describes a systematic survey of the data available in the Protein Data Bank. Several interesting observations could be made. (1) As a...

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Bibliographic Details
Published in:Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2024-04, Vol.92 (4), p.464-473
Main Author: Carugo, Oliviero
Format: Article
Language:English
Subjects:
Cysteine - chemistry
Helices
Oxidation
Oxidation-Reduction
Oxygen
Proteins
Proteins - chemistry
Radiation damage
Structural members
Sulfhydryl Compounds - metabolism
Sulfonic acid
Sulfur
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Summary:Although S-nitrosylation of cysteines is a common protein posttranslational modification, little is known about its three-dimensional structural features. This paper describes a systematic survey of the data available in the Protein Data Bank. Several interesting observations could be made. (1) As a result of radiation damage, S-nitrosylated cysteines (Snc) are frequently reduced, at least partially. (2) S-nitrosylation may be a protection against irreversible thiol oxidation; because the NO group of Snc is relatively accessible to the solvent, it may act as a cork to protect the sulfur atoms of cysteines from oxidation by molecular oxygen to sulfenic, sulfinic, and sulfonic acid; moreover, Snc are frequently found at the start or end of helices and strands and this might shield secondary structural elements from unfolding.
ISSN:0887-3585
1097-0134
DOI:10.1002/prot.26629