4ANR

Crystal structure of soluble lytic Transglycosylase SltB1 from Pseudomonas aeruginosa

4ANR の概要

• エントリーDOI: 10.2210/pdb4anr/pdb
• 分子名称: SOLUBLE LYTIC TRANSGLYCOSYLASE B, CALCIUM ION (3 entities in total)
• 機能のキーワード: lyase, ef-hand like motif, peptidoglycan
• 由来する生物種: PSEUDOMONAS AERUGINOSA
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36403.85

構造登録者

Nikolaidis, I.,Izore, T.,Job, V.,Thielens, N.,Breukink, E.,Dessen, A. (登録日: 2012-03-22, 公開日: 2012-04-04, 最終更新日: 2023-12-20)

主引用文献

Nikolaidis, I.,Izore, T.,Job, V.,Thielens, N.,Breukink, E.,Dessen, A.
Calcium-Dependent Complex Formation between Pbp2 and Lytic Transglycosylase Sltb1 of Pseudomonas Aeruginosa.
Microb.Drug Resist., 18:298-, 2012

PubMed Abstract: In Gram-negative bacteria, the bacterial cell wall biosynthetic mechanism requires the coordinated action of enzymes and structural proteins located in the cytoplasm, within the membrane, and in the periplasm of the cell. Its main component, peptidoglycan (PG), is essential for cell division and wall elongation. Penicillin-binding proteins (PBPs) catalyze the last steps of PG biosynthesis, namely the polymerization of glycan chains and the cross-linking of stem peptides, and can be either monofunctional or bifunctional. Their action is coordinated with that of other enzymes essential for cell-wall biosynthesis, such as lytic transglycosylases (LT). Here, we have studied SltB1, an LT from Pseudomonas aeruginosa, and identified that it forms a complex with PBP2, a monofunctional enzyme, which requires the presence of Ca(2+). In addition, we have solved the structure of SltB1 to a high resolution, and identified that it harbors an EF-hand like motif containing a Ca(2+) ion displaying bipyramidal coordination. These studies provide initial structural details that shed light on the interactions between the PG biosynthesis enzymes in P. aeruginosa.

PubMed: 22432706
DOI: 10.1089/MDR.2012.0006

実験手法

X-RAY DIFFRACTION (1.84 Å)