S-Sulfhydration of the Catalytic Cysteine in the Rhodanese Domain of YgaP is Complex Dynamic Process
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2016-02-20
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Journal Article
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Abstract
The S-sulfhydration of cysteine residues in proteins has emerged as a common modifi cation that can modulate the activity of a protein. The ubiquity of the rhodanese domain and its occurrence in a wide variety of protein families indicates that it has diverse roles in physiology. Contrary to common expectations, previous structural studies of several rhodanese domains concluded that S-sulfhydration does not induce a structural change in the protein. The presented x-ray structure of a thiosulfate- treated crystal of the rho danese domain of the E. coli integral membrane protein YgaP reveals two important findings: (1) The S-sulfhydrated catalytic cysteine C63 adopts an atypical conformation. (2) S-sulfhydration leads to a destabilization of the N-terminal part of the helix adjacent to the catalytic loop. These findings assert that S-sulfhydration is accompanied by a specific and complex dynamic process.
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Sciencematters
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Protein Structure; Tertiary; Protein Processing; Post-Translational
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03782 - Riek, Roland / Riek, Roland