Structural highlights
Publication Abstract from PubMedPoly((R)-3-hydroxybutyrate) (PHB) is a microbial biopolymer widely used in commercial biodegradable plastics. PHB degradation in cell is catalyzed by PHB depolymerase (PhaZ), which hydrolyzes the polyester into mono- and/or oligomeric (R)-3-hydroxylbutyrates (3HB). A novel intracellular PhaZ from Bacillus thuringiensis (BtPhaZ) was identified for potential applications in polymer biodegradation and 3HB production. Herein, we present the crystal structure of BtPhaZ at 1.42-A resolution, making the first crystal structure for an intracellular PhaZ. BtPhaZ comprises a canonical alpha/beta hydrolase catalytic domain and a unique alpha-helical cap domain. Despite lacking sequence similarity, BtPhaZ shares high structural homology with many alpha/beta hydrolase members, exhibiting a similar active-site architecture. Alongside the most conserved superfamily signature, several new conserved signatures have been identified, contributing not only to the formations of the Ser-His-Asp catalytic triad and the oxyanion hole but also to the active-site conformation. The putative P-1 subsite appears to have limited space for accommodating only one 3HB-monomer, which may provide an explanation why the major hydrolytic product for BtPhaZ is monomeric form. Furthermore, a cluster of solvent-exposed hydrophobic residues in the helical cap domain forms an adsorption site for polymer-binding. Detailed structural comparisons reveal that various PhaZs employ distinct residues for the biopolymer-binding and hydrolysis. Structural insight into the poly(3-hydroxybutyrate) hydrolysis by intracellular PHB depolymerase from Bacillus thuringiensis.,Wang YL, Ye LC, Chang SC, Chen SC, Hsu CH Int J Biol Macromol. 2024 Nov 24;284(Pt 1):137999. doi: , 10.1016/j.ijbiomac.2024.137999. PMID:39592048[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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