8DAJ
Structure and Biochemistry of a Promiscuous Thermophilic Polyhydroxybutyrate Depolymerase from Lihuaxuella thermophilia
Summary for 8DAJ
| Entry DOI | 10.2210/pdb8daj/pdb |
| Descriptor | Esterase, PHB depolymerase family, 1,2-ETHANEDIOL, ISOPROPYL ALCOHOL, ... (4 entities in total) |
| Functional Keywords | bioplastic, thermophile, enzyme, polyhydroxyalkanoates, biosynthetic protein |
| Biological source | Lihuaxuella thermophila |
| Total number of polymer chains | 1 |
| Total formula weight | 33302.93 |
| Authors | Thomas, G.M.,Quirk, S.,Huard, D.J.E.,Lieberman, R.L. (deposition date: 2022-06-13, release date: 2023-02-15, Last modification date: 2024-10-23) |
| Primary citation | Thomas, G.M.,Quirk, S.,Huard, D.J.E.,Lieberman, R.L. Bioplastic degradation by a polyhydroxybutyrate depolymerase from a thermophilic soil bacterium. Protein Sci., 31:e4470-e4470, 2022 Cited by PubMed Abstract: As the epidemic of single-use plastic worsens, it has become critical to identify fully renewable plastics such as those that can be degraded using enzymes. Here we describe the structure and biochemistry of an alkaline poly[(R)-3-hydroxybutyric acid] (PHB) depolymerase from the soil thermophile Lihuaxuella thermophila. Like other PHB depolymerases or PHBases, the Lihuaxuella enzyme is active against several different polyhydroxyalkanoates, including homo- and heteropolymers, but L. thermophila PHB depolymerase (LtPHBase) is unique in that it also hydrolyzes polylactic acid and polycaprolactone. LtPHBase exhibits optimal activity at 70°C, and retains 88% of activity upon incubation at 65°C for 3 days. The 1.2 Å resolution crystal structure reveals an α/β-hydrolase fold typical of PHBases, but with a shallow active site containing the catalytic Ser-His-Asp-triad that appears poised for broad substrate specificity. LtPHBase holds promise for the depolymerization of PHB and related bioplastics at high temperature, as would be required in bioindustrial operations like recycling or landfill management. PubMed: 36222314DOI: 10.1002/pro.4470 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
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