I
Ingrid Zegers
Researcher at Vrije Universiteit Brussel
Publications - 25
Citations - 725
Ingrid Zegers is an academic researcher from Vrije Universiteit Brussel. The author has contributed to research in topics: RNase P & Active site. The author has an hindex of 13, co-authored 25 publications receiving 693 citations. Previous affiliations of Ingrid Zegers include Université catholique de Louvain & Free University of Brussels.
Papers
More filters
Journal ArticleDOI
The structures of RNase A complexed with 3'-CMP and d(CpA): active site conformation and conserved water molecules.
TL;DR: The comparison of the present RNase A structures with an inhibitor complex of RNase T1 shows that there are important similarities in the active sites of these 2 enzymes, despite the absence of any sequence homology.
Journal ArticleDOI
Arsenate reductase from S. aureus plasmid pI258 is a phosphatase drafted for redox duty
TL;DR: Results provide evidence that ArsC from pI258 evolved from LMW PTPase by the grafting of a redox function onto a pre-existing catalytic site and that its evolutionary origin is different from those of arsenate reductases from Escherichia coli plasmid R773 and from Saccharomyces cerevisiae.
Journal ArticleDOI
All intermediates of the arsenate reductase mechanism, including an intramolecular dynamic disulfide cascade.
Joris Messens,José C. Martins,Karolien Van Belle,Elke Brosens,Aline Desmyter,Marjan De Gieter,Jean-Michel Wieruszeski,Rudolph Willem,Lode Wyns,Ingrid Zegers +9 more
TL;DR: The mechanism of pI258 arsenate reductase (ArsC) catalyzed arsenate reduction, involving its P-loop structural motif and three redox active cysteines, has been unraveled and Steady-state kinetics of ArsC mutants gives a view of the crucial residues for catalysis.
Journal ArticleDOI
Trimeric domain-swapped barnase
TL;DR: The structure of a trimeric domain-swapped form of barnase (EC 3.3) was determined by x-ray crystallography at a resolution of 2.2 A from crystals of space group R32 and contains three protein folds that are very similar to those in monomeric barnase.
Journal ArticleDOI
Crystal structure of RNase T1 with 3'-guanylic acid and guanosine.
TL;DR: A modified method for the synthesis and separation of endo and exo guanosine 2',3'-cyclophosphorothioate (cGPS) has been developed and the exo diastereoisomer has been co-crystallized with RNase T1.