5Z6H
Structure of periplasmic trehalase from Diamondback moth gut bacteria in the apo form
Summary for 5Z6H
| Entry DOI | 10.2210/pdb5z6h/pdb |
| Related | 5Z66 |
| Descriptor | Periplasmic trehalase, SULFATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | trehalase from insect gut bacterium, apo structure, hydrolase |
| Biological source | Enterobacter cloacae |
| Total number of polymer chains | 2 |
| Total formula weight | 127479.87 |
| Authors | Harne, S.R.,Adhav, A.S.,Joshi, R.S.,Gayathri, P. (deposition date: 2018-01-22, release date: 2019-01-23, Last modification date: 2024-11-06) |
| Primary citation | Adhav, A.,Harne, S.,Bhide, A.,Giri, A.,Gayathri, P.,Joshi, R. Mechanistic insights into enzymatic catalysis by trehalase from the insect gut endosymbiont Enterobacter cloacae. Febs J., 286:1700-1716, 2019 Cited by PubMed Abstract: Energy metabolism in the diamondback moth Plutella xylostella is facilitated by trehalase, an enzyme which assists in trehalose hydrolysis, from the predominant gut bacterium Enterobacter cloacae. We report the biochemical and structural characterization of recombinant trehalase from E. cloacae (Px_EclTre). Px_EclTre showed K of 1.47 (±0.05) mm, k of 6254.72 min and V 0.2 (±0.002) mm·min at 55 °C and acidic pH. Crystal structures of Px_EclTre were determined in the ligand-free form and bound to the inhibitor Validoxylamine A. The crystal structure of the ligand-free form, unavailable until now for any other bacterial trehalases, enabled us to delineate the conformational changes accompanying ligand binding in trehalases. Multiple salt bridges were identified that potentially facilitated closure of a hood over the substrate-binding site. A cluster of five tryptophans lined the -1 substrate-binding subsite, interacted with crucial active site residues and contributed to both trehalase activity and stability. The importance of these residues in enzyme activity was further validated by mutagenesis studies. Many of these identified residues form part of signature motifs and other conserved sequences in trehalases. The structure analysis thus led to the assignment of the functional role to these conserved residues. This information can be further explored for the design of effective inhibitors against trehalases. PubMed: 30657252DOI: 10.1111/febs.14760 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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