Interdomain flexibility and putative active site was revealed by crystal structure of MltG from Acinetobacter baumannii.
Biochem Biophys Res Commun
; 727: 150318, 2024 Oct 01.
Article
em En
| MEDLINE
| ID: mdl-38945066
ABSTRACT
MltG, positioned within the inner membrane of bacteria, functions as a lytic transglycosylase (LT) essential for integrating into the cell wall by cleaving the newly synthesized glycan strand, emphasizing its critical involvement in bacterial cell wall biosynthesis and remodeling. Current study reported the first structure of MltG family of LT. We have elucidated the structure of MltG from Acinetobacter baumannii (abMltG), a formidable superbug renowned for its remarkable antibiotic resistance. Our structural and biochemical investigations unveiled the presence of a flexible peptidoglycan (PG)-binding domain (PGD) within MltG family, which exists as a monomer in solution. Furthermore, we delineated the putative active site of abMltG via a combination of structural analysis and sequence comparison. This discovery enhances our comprehension of the transglycosylation process mediated by the MltG family, offering insights that could inform the development of novel antibiotics tailored to combat A. baumannii.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
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Modelos Moleculares
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Domínio Catalítico
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Acinetobacter baumannii
Idioma:
En
Ano de publicação:
2024
Tipo de documento:
Article