ArticleThe journal of physical chemistry. B2025
A Putative Interaction between the Transmembrane Domains of
Article in The journal of physical chemistry. B, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Sortase enzymes are cysteine transpeptidases at the cell surface of Gram-positive bacteria. Localized to distinct foci on the cell membrane, class A sortases (SrtAs) recognize a cell wall sorting signal (CWSS), and, following cleavage at this specific binding motif, target proteins are ligated to precursors of the growing peptidoglycan layer. This activity of SrtA enzymes is utilized extensively in sortase-mediated ligation (SML) strategies for a variety of protein engineering applications. Typically, engineered variants of SrtA are used for SML experiments, considering the relatively low catalytic efficiency of this enzyme. Understandably, most biochemical studies are conducted with the isolated catalytic domain of SrtA enzymes from various bacteria, and the stereochemistry of the endogenous interaction between SrtA and its substrate is not well understood. Here, we used AlphaFold2 to create a model of the full-length SrtA enzyme from
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