5BX9
Structure of PslG from Pseudomonas aeruginosa
Summary for 5BX9
| Entry DOI | 10.2210/pdb5bx9/pdb |
| Related | 5BXA |
| Descriptor | PslG, CADMIUM ION, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | gh39, glycosidase, hydrolase, alpha beta barrel |
| Biological source | Pseudomonas aeruginosa |
| Total number of polymer chains | 1 |
| Total formula weight | 48114.08 |
| Authors | Baker, P.,Little, D.J.,Howell, P.L. (deposition date: 2015-06-08, release date: 2015-10-07, Last modification date: 2024-03-06) |
| Primary citation | Baker, P.,Whitfield, G.B.,Hill, P.J.,Little, D.J.,Pestrak, M.J.,Robinson, H.,Wozniak, D.J.,Howell, P.L. Characterization of the Pseudomonas aeruginosa Glycoside Hydrolase PslG Reveals That Its Levels Are Critical for Psl Polysaccharide Biosynthesis and Biofilm Formation. J.Biol.Chem., 290:28374-28387, 2015 Cited by PubMed Abstract: A key component of colonization, biofilm formation, and protection of the opportunistic human pathogen Pseudomonas aeruginosa is the biosynthesis of the exopolysaccharide Psl. Composed of a pentameric repeating unit of mannose, glucose, and rhamnose, the biosynthesis of Psl is proposed to occur via a Wzx/Wzy-dependent mechanism. Previous genetic studies have shown that the putative glycoside hydrolase PslG is essential for Psl biosynthesis. To understand the function of this protein, the apo-structure of the periplasmic domain of PslG (PslG(31-442)) and its complex with mannose were determined to 2.0 and 1.9 Å resolution, respectively. Despite a domain architecture and positioning of catalytic residues similar to those of other family 39 glycoside hydrolases, PslG(31-442) exhibits a unique 32-Å-long active site groove that is distinct from other structurally characterized family members. PslG formed a complex with two mannose monosaccharides in this groove, consistent with binding data obtained from intrinsic tryptophan fluorescence. PslG was able to catalyze the hydrolysis of surface-associated Psl, and this activity was abolished in a E165Q/E276Q double catalytic variant. Surprisingly, P. aeruginosa variants with these chromosomal mutations as well as a pslG deletion mutant were still capable of forming Psl biofilms. However, overexpression of PslG in a pslG deletion background impaired biofilm formation and resulted in less surface-associated Psl, suggesting that regulation of this enzyme is important during polysaccharide biosynthesis. PubMed: 26424791DOI: 10.1074/jbc.M115.674929 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.001 Å) |
Structure validation
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