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• W2087598230 abstract "A unique feature of the class-C-type sortases, enzymes essential for Gram-positive pilus biogenesis, is the presence of a flexible lid anchored in the active site. However, the mechanistic details of the lid displacement, suggested to be a critical prelude for enzyme catalysis, are not yet known. This is partly due to the absence of enzyme-substrate and enzyme-inhibitor complex crystal structures. We have recently described the crystal structures of the Streptococcus agalactiae SAG2603 V/R sortase SrtC1 in two space groups (type II and type III) and that of its lid mutant and proposed a role of the lid as a protector of the active-site hydrophobic environment. Here, we report the crystal structures of SAG2603 V/R sortase C1 in a different space group (type I) and that of its complex with a small-molecule cysteine protease inhibitor. We observe that the catalytic Cys residue is covalently linked to the small-molecule inhibitor without lid displacement. However, the type I structure provides a view of the sortase SrtC1 lid displacement while having structural elements similar to a substrate sorting motif suitably positioned in the active site. We propose that these major conformational changes seen in the presence of a substrate mimic in the active site may represent universal features of class C sortase substrate recognition and enzyme activation." @default.
• W2087598230 created "2016-06-24" @default.
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• W2087598230 date "2011-12-01" @default.
• W2087598230 modified "2023-09-24" @default.
• W2087598230 title "The Crystal Structure Analysis of Group B Streptococcus Sortase C1: A Model for the “Lid” Movement upon Substrate Binding" @default.
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• W2087598230 doi "https://doi.org/10.1016/j.jmb.2011.10.017" @default.
• W2087598230 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3230703" @default.
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