4ANR
Crystal structure of soluble lytic Transglycosylase SltB1 from Pseudomonas aeruginosa
Summary for 4ANR
| Entry DOI | 10.2210/pdb4anr/pdb |
| Descriptor | SOLUBLE LYTIC TRANSGLYCOSYLASE B, CALCIUM ION (3 entities in total) |
| Functional Keywords | lyase, ef-hand like motif, peptidoglycan |
| Biological source | PSEUDOMONAS AERUGINOSA |
| Total number of polymer chains | 1 |
| Total formula weight | 36403.85 |
| Authors | Nikolaidis, I.,Izore, T.,Job, V.,Thielens, N.,Breukink, E.,Dessen, A. (deposition date: 2012-03-22, release date: 2012-04-04, Last modification date: 2023-12-20) |
| Primary citation | 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 Cited by 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: 22432706DOI: 10.1089/MDR.2012.0006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.84 Å) |
Structure validation
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