9byu

Structure and stability of an apo thermophilic esterase that hydrolyzes polyhydroxybutyrate

spinqualitylabelsall models 9byu, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9byu is a 1 chain structure with sequence from Lihuaxuella thermophila. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.75Å Ligands: MG, TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1H8IKU3_9BACL Publication Abstract from PubMed Pollution from plastics is a global problem that threatens the biosphere for a host of reasons, including the time scale that it takes for most plastics to degrade. Biodegradation is an ideal solution for remediating bioplastic waste as it does not require the high temperatures necessary for thermal degradation and does not introduce additional pollutants into the environment. Numerous organisms can scavenge for bioplastics, such as polylactic acid (PLA) or poly-(R)-hydroxybutyrate (PHB), which they can use as an energy source. Recently, a promiscuous PHBase from the thermophilic soil bacterium Lihuaxuella thermophila (LtPHBase) was identified. LtPHBase can accommodate many substrates, including PHB granules and films and PHB block copolymers, as well as the unrelated polymers polylactic acid (PLA) and polycaprolactone (PCL). LtPHBase uses the expected Ser-His-Asp catalytic triad for hydrolysis at an optimal enzyme activity near 70 degrees C. Here, the 1.75 A resolution crystal structure of apo LtPHBase is presented and its chemical stability is profiled. Knowledge of its substrate preferences was extended to different-sized PHB granules. It is shown that LtPHBase is highly resistant to unfolding, with barriers typical for thermophilic enzymes, and shows a preference for low-molecular-mass PHB granules. These insights have implications for the long-term potential of LtPHBase as an industrial PHB hydrolase and shed light on the evolutionary role that this enzyme plays in bacterial metabolism. Structure and stability of an apo thermophilic esterase that hydrolyzes polyhydroxybutyrate.,Thomas GM, Quirk S, Lieberman RL Acta Crystallogr D Struct Biol. 2024 Nov 1. doi: 10.1107/S2059798324009707. PMID:39441250 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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