8YQ7

Acinetobacter baumannii membrane-bound lytic murein transglycosylase G

Summary for 8YQ7

• Entry DOI: 10.2210/pdb8yq7/pdb
• Descriptor: Endolytic murein transglycosylase (2 entities in total)
• Functional Keywords: acinetobacter baumannii, membrane-bound lytic murein transglycosylase g, mltg, hydrolase, lyase
• Biological source: Acinetobacter baumannii
• Total number of polymer chains: 6
• Total formula weight: 182031.52

Authors

Jang, H.S.,Park, H.H. (deposition date: 2024-03-19, release date: 2025-03-26, Last modification date: 2025-10-15)

Primary citation

Jang, H.,Kim, C.M.,Ha, H.J.,Hong, E.,Park, H.H.
Interdomain flexibility and putative active site was revealed by crystal structure of MltG from Acinetobacter baumannii.
Biochem.Biophys.Res.Commun., 727:150318-150318, 2024

PubMed 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.

PubMed: 38945066
DOI: 10.1016/j.bbrc.2024.150318

Experimental method

X-RAY DIFFRACTION (2.67 Å)