9y33
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Rubredoxin from Pyrococcus Furiosus at 363K, formyl-Methionine N-terminus
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Structural highlights
FunctionRUBR_PYRFU Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. Publication Abstract from PubMedHow does the structure of a protein change as the temperature is raised from cryogenic conditions at 100 K to 393 K? Understanding the structure and dynamics of proteins under environmental extremes is relevant for human health, biotechnological applications, and our search for life elsewhere in the universe. Here we reveal the high temperature crystal structure of a hyperthermophilic (Pyrococcus furiosus) rubredoxin at 393 K (120 degrees C), together with multiple complementary structures down to 100 K. The results are compared with molecular dynamics calculations. Significant changes in H-bonding are observed. Discussions about high-temperature protein structure and stability need to recognize that low temperature structures may not represent the high temperature case. Some Like It Hot -Structural Changes in Extremophile Rubredoxin at 120 degrees C.,Doukov T, Leontyev I, Jenney FE Jr, George D, Cramer SP Angew Chem Int Ed Engl. 2026 Jan 28;65(5):e20302. doi: 10.1002/anie.202520302. , Epub 2025 Nov 24. PMID:41287388[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 08:37, 29 April 2026.