O
Otto Dideberg
Researcher at Centre national de la recherche scientifique
Publications - 183
Citations - 8441
Otto Dideberg is an academic researcher from Centre national de la recherche scientifique. The author has contributed to research in topics: Penicillin binding proteins & Active site. The author has an hindex of 47, co-authored 183 publications receiving 8090 citations. Previous affiliations of Otto Dideberg include Saarland University & University of Liège.
Papers
More filters
Journal ArticleDOI
Standard Numbering Scheme for Class B β-Lactamases
Moreno Galleni,Josette Lamotte-Brasseur,Gian Maria Rossolini,Jim Spencer,Otto Dideberg,Jean-Marie Frère +5 more
TL;DR: This work proposes a scheme developed through a collaborative approach that preserves traditional numbering of catalytically important residues, is adaptable to new variants or enzymes yet to be discovered and includes a variation for genetic and epidemiological applications.
Journal ArticleDOI
The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold.
TL;DR: The 3‐D structure of Bacillus cereus (569/H/9) beta‐lactamase (EC 3.5.6) has been solved and an approximate internal molecular symmetry is found, with a 2‐fold axis passing roughly through the zinc ion and suggesting a possible gene duplication.
Journal ArticleDOI
Penicillin Binding Proteins: key players in bacterial cell cycle and drug resistance processes
TL;DR: Structural, functional and biological features of penicillin-binding proteins, albeit having initially been identified several decades ago, are now being aggressively pursued as highly attractive targets for the development of novel antibiotherapies.
Journal ArticleDOI
The active-site-serine penicillin-recognizing enzymes as members of the Streptomyces R61 DD-peptidase family.
Bernard Joris,J M Ghuysen,Georges Dive,A Renard,Otto Dideberg,Paulette Charlier,Jean-Marie Frère,Judith A. Kelly,J C Boyington,Paul C. Moews +9 more
TL;DR: Though the evolutionary distance may vary considerably, all these penicillin-interactive proteins and domains appear to be members of a single superfamily of active-site-serine enzymes distinct from the classical trypsin or subtilisin families.
Journal ArticleDOI
Update of the Standard Numbering Scheme for Class B β-Lactamases
Gianpiero Garau,I. Garcia-Saez,Carine Bebrone,Christine Anne,Paola Sandra Mercuri,Moreno Galleni,Jean-Marie Frère,Otto Dideberg +7 more
TL;DR: In this article, a standard numbering scheme (BBLN) was proposed to align β-lactamases with known X-ray structures and two ranking scores were calculated: sequence identities of aligned residues and the structural diversity.