Reference : Amino Acid Sequence of the Penicillin-Binding Protein/DD-Peptidase of Streptomyces K15. ...
Scientific journals : Article
Life sciences : Microbiology
http://hdl.handle.net/2268/4312
Amino Acid Sequence of the Penicillin-Binding Protein/DD-Peptidase of Streptomyces K15. Predicted Secondary Structures of the Low Mr Penicillin-Binding Proteins of Class A
English
Palomeque-Messia, Pilar [Université de Liège - ULg > > > > Centre d'Ingénierie des Protéines > > >]
Englebert, Serge [Université de Liège - ULg > > > Centre d'Ingénierie des Protéines > > >]
Leyh-Bouille, Melina [Université de Liège - ULg > > > Centre d'Ingénierie des Protéines > > >]
Nguyen-Distèche, Martine mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Duez, Colette mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Houba, Simone [Université de Liège - ULg > > Centre d'Ingénierie des Protéines > >]
Dideberg, Otto [Université de Liège - ULg > > > Centre d'Ingénierie des Protéines > > >]
Van Beeumen, Jozef [Rijksuniversiteit Gent - RUG > > > > Lab voor Microbiologie en microbiële genetica > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > > > Centre d'Ingénierie des Protéines > > >]
1-Oct-1991
Biochemical Journal
Portland Press
279
Pt 1
223-230
Yes (verified by ORBi)
International
0264-6021
1470-8728
London
United Kingdom
[en] Clonage ; PBP ; DD-peptidase
[en] The low-Mr penicillin-binding protein (PBP)/DD-transpeptidase of Streptomyces K15 is synthesized in the form of a 291-amino acid-residue precursor possessing a cleavable 29-amino acid-residue signal peptide. Sequence-similarity searches and hydrophobic-cluster analysis show that the Streptomyces K15 enzyme, the Escherichia coli PBPs/DD-carboxy-peptidases 5 and 6, the Bacillus subtilis PBP/DD-carboxypeptidase 5 and the spoIIA product (a putative PBP involved in the sporulation of B. subtilis) are structurally related and form a distinct class A of low-Mr PBPs/DD-peptidases. The distribution of the hydrophobic clusters along the amino acid sequences also shows that the Streptomyces K15 PBP, and by extension the other PBPs of class A, have similarity in the polypeptide folding, with the beta-lactamases of class A, with as reference the Streptomyces albus G and Staphylococcus aureus beta-lactamases of known three-dimensional structure. This comparison allows one to predict most of the secondary structures in the PBPs and the amino acid motifs that define the enzyme active sites.
Centre d'Ingénierie des Protéines - CIP
Researchers ; Professionals
http://hdl.handle.net/2268/4312

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