J. Bacteriol., 03 1996, 1774-1775, Vol 178, No. 6
Copyright © 1996, American Society for Microbiology

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 Enterococus hirae

ME Mollerach, P Partoune, J Coyette and JM Ghuysen
Centre d'Ingenierie des Proteines, Institut de Chimie, Universite de Liege, Belgium.

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.

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