Changes in Protein Dynamics in Escherichia coli SufS Reveal a Possible Conserved Regulatory Mechanism in Type II Cysteine Desulfurase Systems.
Sign Up to like & getrecommendations! Published in 2018 at "Biochemistry"
DOI: 10.1021/acs.biochem.7b01275
Abstract: In the Suf Fe-S cluster assembly pathway, the activity of the cysteine desulfurase, SufS, is regulated by interactions with the accessory sulfotransferase protein, SufE. SufE has been shown to stimulate SufS activity, likely by inducing… read more here.
Keywords: dimer interface; cysteine desulfurase; sufs; mechanism ... See more keywords
The Plasmodium falciparum apicoplast cysteine desulfurase provides sulfur for both iron-sulfur cluster assembly and tRNA modification
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DOI: 10.1101/2022.10.31.514511
Abstract: Iron sulfur clusters (FeS) are ancient and ubiquitous protein cofactors that play fundamental roles in many aspects of cell biology. These cofactors cannot be scavenged or trafficked within a cell and thus must be synthesized… read more here.
Keywords: sufs; iron sulfur; cysteine desulfurase; biology ... See more keywords
Structural and Biochemical Characterization of Mycobacterium tuberculosis Zinc SufU-SufS Complex
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DOI: 10.3390/biom13050732
Abstract: Iron-sulfur (Fe-S) clusters are inorganic prosthetic groups in proteins composed exclusively of iron and inorganic sulfide. These cofactors are required in a wide range of critical cellular pathways. Iron-sulfur clusters do not form spontaneously in… read more here.
Keywords: sufs; mycobacterium tuberculosis; tuberculosis; zinc sufu ... See more keywords