1OXC
LecB (PA-LII) in complex with FUCOSE
Summary for 1OXC
| Entry DOI | 10.2210/pdb1oxc/pdb |
| Related | 1GZT 1OUR 1OUS 1OUX 1OVP 1OVS |
| Descriptor | hypothetical protein LecB, beta-L-fucopyranose, alpha-L-fucopyranose, ... (6 entities in total) |
| Functional Keywords | lectin, carbohydrate, sugar binding protein |
| Biological source | Pseudomonas aeruginosa |
| Total number of polymer chains | 4 |
| Total formula weight | 48340.45 |
| Authors | Loris, R.,Tielker, D.,Jaeger, K.-E.,Wyns, L. (deposition date: 2003-04-02, release date: 2003-09-09, Last modification date: 2024-03-13) |
| Primary citation | Loris, R.,Tielker, D.,Jaeger, K.-E.,Wyns, L. Structural Basis of Carbohydrate Recognition by the Lectin LecB from Pseudomonas aeruginosa J.MOL.BIOL., 331:861-870, 2003 Cited by PubMed Abstract: The crystal structure of Pseudomonas aeruginosa fucose-specific lectin LecB was determined in its metal-bound and metal-free state as well as in complex with fucose, mannose and fructopyranose. All three monosaccharides bind isosterically via direct interactions with two calcium ions as well as direct hydrogen bonds with several side-chains. The higher affinity for fucose is explained by the details of the binding site around C6 and O1 of fucose. In the mannose and fructose complexes, a carboxylate oxygen atom and one or two hydroxyl groups are partly shielded from solvent upon sugar binding, preventing them from completely fulfilling their hydrogen bonding potential. In the fucose complex, no such defects are observed. Instead, C6 makes favourable interactions with a small hydrophobic patch. Upon demetallization, the C terminus as well as the otherwise rigid metal-binding loop become more mobile and adopt multiple conformations. PubMed: 12909014DOI: 10.1016/S0022-2836(03)00754-X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
Download full validation report
