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.

Abstract:

: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.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Mollerach ME,Partoune P,Coyette J,Ghuysen JM

doi

10.1128/jb.178.6.1774-1775.1996

subject

Has Abstract

pub_date

1996-03-01 00:00:00

pages

1774-5

issue

6

eissn

0021-9193

issn

1098-5530

journal_volume

178

pub_type

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