{"instituterec":{"StatusID":1,"InsID":14586,"StandardName":"Laboratory of Microbiology","OrigName":null,"OrigNameLangCode":null,"OrigNameLangID":null,"Acronym":"ULB","HigherInsID":14585,"VlizCoreFlag":1,"AdrID":null,"Line1":null,"Line2":null,"Line3":null,"Line4":null,"Phone":null,"GSM":null,"Email":null,"Lat":null,"Lon":null,"OrigNameLang":null,"OrigNameLangNL":null,"AbstractEnglish":"The laboratory of Microbiology studies the following topics: \r\n- 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.
\r\n\r\nWithin 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.","AbstractOtherLang":"Het laboratorium voor Microbiologie bestudeert de volgende onderwerpen: \r\n- fysiologie van mesofiele en thermofiele micro-organismen;
- relaties tussen structuur en functie in proteïnen en enzymen;
- biosynthese en functie van de gewijzigde nucleosiden van transfer-RNA.
\r\n\r\nOp marien gebied bestudeert de groep het enzym M42 aminopeptidase in de thermofiele bacterie Thermotoga maritima, oorspronkelijk geïsoleerd uit een diepzee hydrothermale bron. De groep richt zich op de overgang van de oligomere toestand, de structurele en functionele rol van een geconserveerd aspartaatresidu in de katalytische site, en hoe metaalcofactoren de overgang van dimeer naar dodecameer van het enzym aansturen. Het onderzoek maakt gebruik van röntgenkristallografie en technieken voor eiwitanalyse om de moleculaire kenmerken en mechanismen van dit enzym te onderzoeken.","AbstractLangCode":null,"AbstractLangID":null,"AbstractLang":null,"AbstractLangNL":null,"SuccessorOfInsID":null,"DateLastModified":{"date":"2024-06-04 01:34:19.073000","timezone_type":1,"timezone":"+00:00"},"PrevIns":null,"PrevAcro":null,"PublicFlag":1,"CheckedFlag":0,"ParID":4535,"InstituteType":"Scientific","EnvName":null,"ISO3166":null,"LevelName":null,"ND":"2020-08-19","UD":"2020-09-28","EncAddress":""},"parent":{"PublicFlag":1,"InsID":14585,"OrigNameLangCode":"fr","OrigNameLangID":22,"FullStandardName":"Université Libre de Bruxelles; Faculté des Sciences; Department of Molecular Biology","FullOrigName":"Université Libre de Bruxelles; Faculty of Sciences; Département de Biologie Moléculaire","Acronym":"ULB-DBM"},"institutes":null,"references":[{"BRefID":328340,"RR":"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","PeerRev":1},{"BRefID":328342,"RR":"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","PeerRev":1},{"BRefID":322849,"RR":"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","PeerRev":1}],"conferences":null,"datasets":null,"persons":[{"PersID":38813,"Surname":"Droogmans","Firstname":"Louis","Initials":"L.","DirectorFlag":null,"MarineSciFlag":null,"SpecializedFlag":null,"Function":null},{"PersID":38810,"Surname":"Van Elder","Firstname":"Dany","Initials":"D.","DirectorFlag":null,"MarineSciFlag":null,"SpecializedFlag":null,"Function":null}],"pastpers":null,"subpers":null,"projects":null,"urls":null,"pictures":[],"published":null,"affrefs":null,"collections":null,"thesterms":[{"ThesaurusTerm":"Biochemistry","ThestID":181483,"ThesTypID":29,"ThesType":"MOG Topics"},{"ThesaurusTerm":"Microbiology","ThestID":181509,"ThesTypID":29,"ThesType":"MOG Topics"},{"ThesaurusTerm":"Molecular biology","ThestID":181511,"ThesTypID":29,"ThesType":"MOG Topics"}],"taxterms":null,"geoterms":null,"thestermsFRIS":[{"ThesaurusTerm":"Biochemistry","DutchTerm":"Biochemie","ThestID":181483,"ThesTypID":29,"ThesType":"MOG Topics","Code":null},{"ThesaurusTerm":"Microbiology","DutchTerm":"Microbiologie","ThestID":181509,"ThesTypID":29,"ThesType":"MOG Topics","Code":null},{"ThesaurusTerm":"Molecular biology","DutchTerm":"Moleculaire biologie","ThestID":181511,"ThesTypID":29,"ThesType":"MOG Topics","Code":null}],"nXtins":null,"previns":null,"spcols":[{"SpColID":99,"SpName":"Marine expertise"},{"SpColID":122,"SpName":"Marine expertise: Type: French speaking university"}],"resmessage":"","complete":1,"participantrec":null,"peerrevs":3,"urlmaps":[]}