Author:
Jenney Francis E.,Wang Hongxin,George Simon J.,Xiong Jin,Guo Yisong,Gee Leland B.,Marizcurrena Juan José,Castro-Sowinski Susana,Staskiewicz Anna,Yoda Yoshitaka,Hu Michael Y.,Tamasaku Kenji,Nagasawa Nobumoto,Li Lei,Matsuura Hiroaki,Doukov Tzanko,Cramer Stephen P.
Abstract
AbstractExtremophile organisms are known that can metabolize at temperatures down to − 25 °C (psychrophiles) and up to 122 °C (hyperthermophiles). Understanding viability under extreme conditions is relevant for human health, biotechnological applications, and our search for life elsewhere in the universe. Information about the stability and dynamics of proteins under environmental extremes is an important factor in this regard. Here we compare the dynamics of small Fe-S proteins – rubredoxins – from psychrophilic and hyperthermophilic microorganisms, using three different nuclear techniques as well as molecular dynamics calculations to quantify motion at the Fe site. The theory of ‘corresponding states’ posits that homologous proteins from different extremophiles have comparable flexibilities at the optimum growth temperatures of their respective organisms. Although ‘corresponding states’ would predict greater flexibility for rubredoxins that operate at low temperatures, we find that from 4 to 300 K, the dynamics of the Fe sites in these homologous proteins are essentially equivalent.
Publisher
Springer Science and Business Media LLC
Cited by
2 articles.
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