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

Abstract

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.