ArticleThe Journal of biological chemistry2014
Staphylococcal SplB serine protease utilizes a novel molecular mechanism of activation.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 22 citations in OpenAlex.
- N-terminal processing unlocks global dynamics for substrate engagement in Spl proteases.Science advances · 2026Article
- Staphylococcal SplA and SplB Serine Protease Allelic Variants Exhibit Different Substrate Specificities.Chembiochem : a European journal of chemical biology · 2026Article
- pTripleTREP - A vector for tightly controlled expression and purification of virulence factors in Staphylococcus aureus.Microbial cell factories · 2025Article
- Identifying and controlling inactive and active conformations of a serine protease.Science advances · 2025Article
- Staphylococcal SplA and SplB serine proteases target ubiquitin(-like) specific proteases.AMB Express · 2025Article
- Evolution of protease activation and specificity via alpha-2-macroglobulin-mediated covalent capture.Nature communications · 2023Article
- Dibenzyl (benzo [d] thiazol-2-yl (hydroxy) methyl) phosphonate (DBTMP) showing anti-S. aureus and anti-biofilm properties by elevating activities of serine protease (SspA) and cysteine protease staphopain B (SspB).Archives of microbiology · 2022Article
- The Protease SplB of Staphylococcus aureus Targets Host Complement Components and Inhibits Complement-Mediated Bacterial Opsonophagocytosis.Journal of bacteriology · 2022Article
- Insight into the human pathodegradome of the V8 protease from Staphylococcus aureus.Cell reports · 2021Article
- Structural Determinants of Substrate Specificity of SplF Protease fromInternational journal of molecular sciences · 2021Article
- Structural insights into the role of the N-terminus in the activation and function of extracellular serine protease from Staphylococcus epidermidis.Acta crystallographica. Section D, Structural biology · 2020Article
- Heterologous Expression of the Class IIa Bacteriocins, Plantaricin 423 and Mundticin ST4SA, inFrontiers in microbiology · 2020Article
- Proteolytic processing and activation of gingipain zymogens secreted by T9SS of Porphyromonas gingivalis.Biochimie · 2019Article
- A versatile modular vector set for optimizing protein expression among bacterial, yeast, insect and mammalian hosts.PloS one · 2019Article
- Transcript Profiling of MRSA Biofilms Treated with a Halogenated Phenazine Eradicating Agent: A Platform for Defining Cellular Targets and Pathways Critical to Biofilm Survival.Angewandte Chemie (International ed. in English) · 2018Article
Corrections and comments
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Authors and funding
14 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Staphylococcal SplB protease belongs to the chymotrypsin family. Chymotrypsin zymogen is activated by proteolytic processing at the N terminus, resulting in significant structural rearrangement at the active site. Here, we demonstrate that the molecular mechanism of SplB protease activation differs significantly and we characterize the novel mechanism in detail. Using peptide and protein substrates we show that the native signal peptide, or any N-terminal extension, has an inhibitory effect on SplB. Only precise N-terminal processing releases the full proteolytic activity of the wild type analogously to chymotrypsin. However, comparison of the crystal structures of mature SplB and a zymogen mimic show no rearrangement at the active site whatsoever. Instead, only the formation of a unique hydrogen bond network, distant form the active site, by the new N-terminal glutamic acid of mature SplB is observed. The importance of this network and influence of particular hydrogen bond interactions at the N terminus on the catalytic process is demonstrated by evaluating the kinetics of a series of mutants. The results allow us to propose a consistent model where changes in the overall protein dynamics rather than structural rearrangement of the active site are involved in the activation process.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.