ArticleThe Journal of biological chemistry2012
Ultrahigh and high resolution structures and mutational analysis of monomeric Streptococcus pyogenes SpeB reveal a functional role for the glycine-rich C-terminal loop.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Review
- Functional insights from recombinant production of bacterial proteases in Saccharomyces cerevisiae.Microbial cell factories · 2025Article
- Proinflammatory synergy between protease and superantigen streptococcal pyogenic exotoxins.Infection and immunity · 2025Article
- Immunomodulating Enzymes fromMicroorganisms · 2024Review
- Proteolytic Profiling of Streptococcal Pyrogenic Exotoxin B (SpeB) by Complementary HPLC-MS Approaches.International journal of molecular sciences · 2021Article
- Kirkwood-Buff-Derived Force Field for Peptides and Proteins: Applications of KBFF20.Journal of chemical theory and computation · 2021Article
- An Irreversible Inhibitor to Probe the Role ofACS chemical biology · 2020Article
- Sulfur(VI) Fluoride Exchange (SuFEx)-Enabled High-Throughput Medicinal Chemistry.Journal of the American Chemical Society · 2020Article
- Highly efficient recombinant production and purification of streptococcal cysteine protease streptopain with increased enzymatic activity.Protein expression and purification · 2016Article
- Article
- Metal-mediated modulation of streptococcal cysteine protease activity and its biological implications.Infection and immunity · 2014Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cysteine protease SpeB is secreted from Streptococcus pyogenes and has been studied as a potential virulence factor since its identification almost 70 years ago. Here, we report the crystal structures of apo mature SpeB to 1.06 Å resolution as well as complexes with the general cysteine protease inhibitor trans-epoxysuccinyl-l-leucylamido(4-guanidino)butane and a novel substrate mimetic peptide inhibitor. These structures uncover conformational changes associated with maturation of SpeB from the inactive zymogen to its active form and identify the residues required for substrate binding. With the use of a newly developed fluorogenic tripeptide substrate to measure SpeB activity, we determined IC(50) values for trans-epoxysuccinyl-l-leucylamido(4-guanidino)butane and our new peptide inhibitor and the effects of mutations within the C-terminal active site loop. The structures and mutational analysis suggest that the conformational movements of the glycine-rich C-terminal loop are important for the recognition and recruitment of biological substrates and release of hydrolyzed products.
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