ArticleThe Journal of biological chemistry2009
Solution structure and backbone dynamics of streptopain: insight into diverse substrate specificity.
Article in The Journal of biological chemistry, 2009. 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, 22 citations in OpenAlex.
- Proinflammatory synergy between protease and superantigen streptococcal pyogenic exotoxins.Infection and immunity · 2025Article
- C10Pred: A First Machine Learning Based Tool to Predict C10 Family Cysteine Peptidases Using Sequence-Derived Features.International journal of molecular sciences · 2022Article
- Evolution of Streptococcus pyogenes has maximized the efficiency of the Sortase A cleavage motif for cell wall transpeptidation.The Journal of biological chemistry · 2022Article
- Proteolytic Profiling of Streptococcal Pyrogenic Exotoxin B (SpeB) by Complementary HPLC-MS Approaches.International journal of molecular sciences · 2021Article
- Highly efficient recombinant production and purification of streptococcal cysteine protease streptopain with increased enzymatic activity.Protein expression and purification · 2016Article
- Metal-mediated modulation of streptococcal cysteine protease activity and its biological implications.Infection and immunity · 2014Article
- Determining antibody-binding site of streptococcal pyrogenic exotoxin B to protect mice from group a streptococcus infection.PloS one · 2013Article
- Mapping inhibitor binding modes on an active cysteine protease via nuclear magnetic resonance spectroscopy.Biochemistry · 2012Article
- Ultrahigh and high resolution structures and mutational analysis of monomeric Streptococcus pyogenes SpeB reveal a functional role for the glycine-rich C-terminal loop.The Journal of biological chemistry · 2012Article
- Functional insight into the C-terminal extension of halolysin SptA from haloarchaeon Natrinema sp. J7.PloS one · 2011Article
- Functional aspects of protein flexibility.Cellular and molecular life sciences : CMLS · 2009Review
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Streptococcal pyrogenic exotoxin B (SPE B) is a cysteine protease expressed by Streptococcus pyogenes. The D9N, G163S, G163S/A172S, and G239D mutant proteins were expressed to study the effect of the allelic variants on their protease activity. In contrast to other mutants, the G239D mutant was approximately 12-fold less active. The Gly-239 residue is located within the C-terminal S230-G239 region, which cannot be observed in the x-ray structure. The three-dimensional structure and backbone dynamics of the 28-kDa mature SPE B (mSPE B) were determined. Unlike the x-ray structure of the 40-kDa zymogen SPE B (proSPE B), we observed the interactions between the C-terminal loop and the active site residues in mSPE B. The structural differences between mSPE B and proSPE B were the conformation of the C-terminal loop and the orientation of the catalytic His-195 residue, suggesting that activation and inactivation of SPE B is involved in the His-195 side-chain rotation. Dynamics analysis of mSPE B and the mSPE B/inhibitor complexes showed that the catalytic and C-terminal loops were the most flexible regions with low order parameter values of 0.5 to 0.8 and exhibited the motion on the ps/ns timescale. These findings suggest that the flexible C-terminal loop of SPE B may play an important role in controlling the substrate binding, resulting in its broad substrate specificity.
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