8slv

Structure of a salivary alpha-glucosidase from the mosquito vector Aedes aegypti.Structure of a salivary alpha-glucosidase from the mosquito vector Aedes aegypti.

Structural highlights 8slv is a 1 chain structure with sequence from Aedes aegypti. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.32Å Ligands: , , , , , , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MALT_AEDAE Assists the mosquito in its sugar-feeding capabilities (Potential). Glucosidase (By similarity). Publication Abstract from PubMed Mosquito vectors of medical importance both blood and sugar feed, and their saliva contains bioactive molecules that aid in both processes. Although it has been shown that the salivary glands of several mosquito species exhibit alpha-glucosidase activities, the specific enzymes responsible for sugar digestion remain understudied. We therefore expressed and purified three recombinant salivary alpha-glucosidases from the mosquito vectors Aedes aegypti, Anopheles gambiae, and Culex quinquefasciatus and compared their functions and structures. We found that all three enzymes were expressed in the salivary glands of their respective vectors and were secreted into the saliva. The proteins, as well as mosquito salivary gland extracts, exhibited alpha-glucosidase activity, and the recombinant enzymes displayed preference for sucrose compared to p-nitrophenyl-alpha-D-glucopyranoside. Finally, we solved the crystal structure of the Ae. aegypti alpha-glucosidase bound to two calcium ions at a 2.3 Angstrom resolution. Molecular docking suggested that the Ae. aegypti alpha-glucosidase preferred di- or polysaccharides compared to monosaccharides, consistent with enzymatic activity assays. Comparing structural models between the three species revealed a high degree of similarity, suggesting similar functional properties. We conclude that the alpha-glucosidases studied herein are important enzymes for sugar digestion in three mosquito species. Structural and functional comparisons of salivary alpha-glucosidases from the mosquito vectors Aedes aegypti, Anopheles gambiae, and Culex quinquefasciatus.,Williams AE, Gittis AG, Botello K, Cruz P, Martin-Martin I, Valenzuela Leon PC, Sumner B, Bonilla B, Calvo E Insect Biochem Mol Biol. 2024 Apr;167:104097. doi: 10.1016/j.ibmb.2024.104097. , Epub 2024 Feb 28. PMID:38428508 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 8slv, resolution 2.32Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image