A5050417314- Bacterial Genetics and Biotechnology
- Enzyme Structure and Function
- Protein Structure and Dynamics
- Vibrio bacteria research studies
- Antibiotic Resistance in Bacteria
- RNA and protein synthesis mechanisms
- Bacteriophages and microbial interactions
- Escherichia coli research studies
- Antimicrobial Resistance in Staphylococcus
- Bacillus and Francisella bacterial research
- Toxin Mechanisms and Immunotoxins
- Phytase and its Applications
- Phytochemical compounds biological activities
- Enzyme Production and Characterization
- Cancer therapeutics and mechanisms
- Fungal and yeast genetics research
- Plant Gene Expression Analysis
- Photosynthetic Processes and Mechanisms
- Mass Spectrometry Techniques and Applications
Vrije Universiteit Brussel
2009-2025
VIB-VUB Center for Structural Biology
2009-2025
Vlaams Instituut voor Biotechnologie
2014-2017
Abstract Disordered protein sequences can exhibit different binding modes, ranging from well-ordered folding-upon-binding to highly dynamic fuzzy binding. The primary function of the intrinsically disordered region antitoxin HigA2 Vibrio cholerae is neutralize HigB2 toxin through ultra-high-affinity interaction. Here, we show that same also mediate interactions with its operator DNA and, interplay folded helix-turn-helix domain, regulates transcription higBA2 operon. NMR, SAXS, ITC and in...
Toxin-antitoxin (TA) modules are small operons involved in bacterial stress response and persistence. higBA form a family of TA with an inverted gene organization toxin belonging to the RelE/ParE superfamily. Here, we present crystal structures chromosomally encoded Vibrio cholerae antitoxin (VcHigA2), (VcHigB2) their complex, which show significant differences structure mechanisms function compared module from plasmid Rts1, defining member family. The VcHigB2 is more closely related...
Intrinsically disordered proteins (IDPs) are that lack a unique three-dimensional structure in their native state. Many have, however, been found to fold into defined when interacting with specific binding partners. The energetic implications of such behavior have widely discussed, yet experimental thermodynamic data is scarce. We present here thorough and structural study the an IDP (antitoxin CcdA) its molecular target (gyrase poison CcdB). show binding-coupled folding CcdA driven by...
The Staphylococcus aureus genome contains three toxin–antitoxin modules, including one mazEF module, SamazEF. Using an on-column separation protocol we are able to obtain large amounts of wild-type SaMazF toxin. protein is well-folded and highly resistant against thermal unfolding but aggregates at elevated temperatures. Crystallographic nuclear magnetic resonance (NMR) solution studies show a well-defined dimer. Differences in structure dynamics between the X-ray NMR structural ensembles...
The latex of the common fig (Ficus carica) contains a mixture at least five cysteine proteases commonly known as ficins (EC 3.4.22.3). Four these were purified to homogeneity and crystals obtained in variety conditions. four ficin (iso)forms appear ten different crystal forms. All diffracted better than 2.10 Å resolution for each form one 1.60 or higher. Ficin B C share form, suggesting close sequence structural similarity. latter 1.20 belonged space group P3₁21 P3₂21, with unit-cell...
Summary Toxin–antitoxin (TA) modules are small operons associated with stress response of bacteria. F‐plasmid CcdB F was the first TA toxin for which its target, gyrase, identified. Plasmidic and chromosomal CcdBs belong to distinct families. Conserved residues crucial gyrase poisoning activity plasmidic not conserved among these Here we show that Vfi from Vibrio fischeri is an active poison interacts target via alternative energetic mechanism. Changes in GyrA14‐binding surface family...
CcdB(Vfi) from Vibrio fischeri is a member of the CcdB family toxins that poison covalent gyrase-DNA complexes. In solution dimer unfolds to corresponding monomeric components in two-state fashion. unfolded state, monomer retains partial secondary structure. This observation correlates well with crystal and NMR structures protein, which show hydrophobic core crossing interface. contrast its F plasmid homologue, possesses rigid interface, apparent relative rotations two subunits are due...
Escherichia coli O157 paaR2-paaA2-parE2 constitutes a unique three-component toxin-antitoxin (TA) module encoding toxin (ParE2) related to the classic parDE family but with an unrelated antitoxin called PaaA2. The complex between PaaA2 and ParE2 was purified characterized by analytical gel filtration, dynamic light scattering small-angle X-ray scattering. It consists of particle radius gyration 3.95 nm is likely form heterododecamer. Crystals ParE2-PaaA2 diffract 3.8 Å resolution belong...
mazEF modules encode toxin-antitoxin pairs that are involved in the bacterial stress response through controlled and specific degradation of mRNA. Staphylococcus aureus MazF MazE constitute a unique module under regulation sigB operon. A MazF-type mRNA interferase is combined with an antitoxin unknown fold. Crystals S. (SaMazF) were grown space group P2(1)2(1)2(1). The crystals diffracted to 2.1 Å resolution likely contain two SaMazF dimers asymmetric unit.
The paaR2 – paaA2 parE2 operon is a three-component toxin–antitoxin module encoded in the genome of human pathogen Escherichia coli O157. toxin (ParE2) and antitoxin (PaaA2) interact to form nontoxic complex. In this paper, crystallization preliminary characterization two variants ParE2–PaaA2 complex are described. Selenomethionine-derivative crystals full-length diffracted 2.8 Å resolution belonged space group P 4 1 2 (or 3 2), with unit-cell parameters = b 90.5, c 412.3 Å. It was...