Research Article The 2.4-Å crystal structure of the penicillin-resistant penicil- lin-binding protein PBP5fm from Enterococcus faecium in complex with benzylpenicillin
作者： F. Kerff , E. Sauvage , R. Herman , P. Charlier , J. Dumas
DOI:
关键词: Benzylpenicillin 、 Penicillin resistant 、 Crystal structure 、 Binding protein 、 Research article 、 Active site 、 Enterococcus faecium 、 Biochemistry 、 Biology
摘要: Penicillin-binding proteins (PBPs) are mem- brane involved in the final stages of peptidogly- can synthesis and represent targets b-lactam an- tibiotics. Enterococci naturally resistant to these tibiotics because they produce a PBP, named PBP5fm Enterococcus faecium, with low-level affinity for b-lac- tams. We report here crystal structure acyl-en- zyme complex benzylpenicillin at res- olution 2.4 A. A characteristic active site, which distinguishes from other PBPs known struc- ture, is topology loop 451-465 defining left
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