Parent institute: Université Libre de Bruxelles; Faculté des Sciences; Department of Molecular Biology (ULB-DBM), more
MRG keywords (3) : Biochemistry; Microbiology; Molecular biology
Type: Scientific
| |
1 Director: Head of the department 2 Marine scientist: Works in this research group and acts as (co-)author in at least one marine publication in the last 5 years. 3 Specialized personnel: Provides administrative or technical support to marine scientific research.
| Abstract: | The laboratory of Microbiology studies the following topics:
- physiology of mesophilic and thermophilic microorganisms;
- relationships between structure and function in proteins and enzymes;
- biosynthesis and function of the modified nucleosides of transfer RNA.
Within the marine field, the group studies the M42 aminopeptidase enzyme in the thermophilic bacterium Thermotoga maritima, originally isolated from a deep-sea hydrothermal vent. The group focuses on its oligomeric state transition, the structural and functional role of a conserved aspartate residue in the catalytic site, and how metal cofactors drive the dimer-dodecamer transition of the enzyme. The research utilises X-ray crystallography and protein analysis techniques to investigate the molecular characteristics and mechanisms of this enzyme. |
| Publications (3) | Top | Persons | ( 3 peer reviewed ) split up filter Dutoit, R.; Brandt, N.; Van Elder, D.; Droogmans, L. (2020). X-ray crystallography to study the oligomeric state transition of the Thermotoga maritima M42 aminopeptidase TmPep1050. Jove-Journal of Visualized Experiments 159: e61288. https://dx.doi.org/10.3791/61288, more- Dutoit, R.; Brandt, N.; Van Gompel, T.; Van Elder, D.; Van Dyck, J.; Sobott, F.; Droogmans, L. (2020). M42 aminopeptidase catalytic site: the structural and functional role of a strictly conserved aspartate residue. Proteins-Structure Function and Bioinformatics 88(12): 1639-1647. https://dx.doi.org/10.1002/prot.25982, more
- Dutoit, R.; Van Gompel, T.; Brandt, N.; Van Elder, D.; Van Dyck, J.; Sobott, F.; Droogmans, L. (2019). How metal cofactors drive dimer–dodecamer transition of the M42 aminopeptidase TmPep1050 of Thermotoga maritima. J. Biol. Chem. 294(47): 17777-17789. https://dx.doi.org/10.1074/jbc.RA119.009281, more
|
|
