Importance of the E46-D160 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.

MOLLERACH M; PARTOUNE P; COYETTE J; GHUYSEN JM

JOURNAL OF BACTERIOLOGY

American Society for Microbiology

Año: 1996 vol. 178 p. 1774 - 1775

0021-9193

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.