RNase Y is a crucial component of genetic translation, acting as the key enzyme initiating mRNA decay in many Gram-positive bacteria. The N-terminal domain of Bacillus subtilis RNase Y (Nter-BsRNaseY) is thought to interact with various protein partners within a degradosome complex. Bioinformatics and biophysical analysis have previously shown that Nter-BsRNaseY, which is in equilibrium between a monomeric and a dimeric form, displays an elongated fold with a high content of ?-helices. Using...
Using Tryptophan Mutants To Probe the Structural andFunctional Status of BsSCO, a Copper Binding, Cytochrome c Oxidase Assembly Protein from Bacillus subtilis
Using Tryptophan Mutants To Probe the Structural andFunctional Status of BsSCO, a Copper Binding, Cytochrome c Oxidase Assembly Protein from Bacillus subtilis
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00833/20171117/images/medium/bi-2017-00833p_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00833
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Eur J...
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Structural Insights into the Dimeric Form of Bacillus subtilis RNase Y Using NMR and AlphaFold
Linear Mode
