Reference : Importance of the E-46-D-160 Polypeptide Segment of the Non-Penicillin-Binding Module fo...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/90901
Importance of the E-46-D-160 Polypeptide Segment of the Non-Penicillin-Binding Module for the Folding of the Low-Affinity, Multimodular Class B Penicillin-Binding Protein 5 of Enterococcus Hirae
English
Mollerach, Marta E. [Madrid > Departamento de Microbiologia Molecular > Centro de Investigaciones Biologicas > >]
Partoune, Pierre [Madrid > Departamento de Microbiologia Molecular > Centro de Investigaciones Biologicas > >]
Coyette, Jacques [Université de Liège - ULg > Institut de Chimie > Centre d'Ingénierie des Protéines > > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Institut de Chimie > Centre d'Ingénierie des Protéines > > >]
Mar-1996
Journal of Bacteriology
American Society for Microbiology (ASM)
178
6
1774-1775
Yes (verified by ORBi)
International
0021-9193
1098-5530
Washington
DC
[en] Compared with the other class B multimodular penicillin- binding proteins (PBPs), the low-affinity PBP5 responsible for penicillin resistance in Enterococcus hirae R40, has an extended non-penicillin-binding module because of the presence of an approximately 110-amino-acid E-46(-)D-160 insert downstream from the membrane anchor. Expression of pbp5 genes lacking various parts of the insert-encoding region gives rise to proteins that are inert in terms of penicillin binding, showing that during folding of the PBP, the insert plays a role in the acquisition of a correct penicillin-binding configuration by the G-364(-)Q-678 carboxy-terminal module.
Centre d'Ingénierie des Protéines - CIP
Fonds de la Recherche Scientifique Médicale - FRSM
Researchers ; Professionals
http://hdl.handle.net/2268/90901

File(s) associated to this reference

Fulltext file(s):

FileCommentaryVersionSizeAccess
Open access
MOLLERACH_1996_multimodular.pdfAuthor postprint185.36 kBView/Open

Bookmark and Share SFX Query

All documents in ORBi are protected by a user license.