7TQR
Crystal Structure of histidine ammonia lyase from Thermoplasma acidophilum
Summary for 7TQR
| Entry DOI | 10.2210/pdb7tqr/pdb |
| Descriptor | Probable histidine ammonia-lyase (2 entities in total) |
| Functional Keywords | histidine ammonia lyase, acid stress, lyase |
| Biological source | Thermoplasma acidophilum |
| Total number of polymer chains | 1 |
| Total formula weight | 54258.73 |
| Authors | Wu, K.,Dulchavsky, M.,Bardwell, J.C.A. (deposition date: 2022-01-26, release date: 2022-04-06, Last modification date: 2024-10-09) |
| Primary citation | Ade, C.,Marcelino, T.F.,Dulchavsky, M.,Wu, K.,Bardwell, J.C.A.,Stadler, B. Microreactor equipped with naturally acid-resistant histidine ammonia lyase from an extremophile. Mater Adv, 3:3649-3662, 2022 Cited by PubMed Abstract: Extremophile enzymes are useful in biotechnology and biomedicine due to their abilities to withstand harsh environments. The abilities of histidine ammonia lyases from different extremophiles to preserve their catalytic activities after exposure to acid were assessed. histidine ammonia lyase was identified as an enzyme with a promising catalytic profile following acid treatment. The fusion of this enzyme with the maltose-binding protein or co-incubation with the chaperone HdeA further helped histidine ammonia lyase to withstand acid treatments down to pH 2.8. The assembly of a microreactor by encapsulation of MBP- histidine ammonia lyase into a photocrosslinked poly(vinyl alcohol) hydrogel allowed the enzyme to recover over 50% of its enzymatic activity following exposure to simulated gastric and intestinal fluids. Our results show that using engineered proteins obtained from extremophiles in combination with polymer-based encapsulation can advance the oral formulations of biologicals. PubMed: 36238657DOI: 10.1039/d2ma00051b PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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