8ynw

S102A mutant of poly(3-hydroxybutyrate) depolymerase PhaZ from Bacillus thuringiensisS102A mutant of poly(3-hydroxybutyrate) depolymerase PhaZ from Bacillus thuringiensis

Structural highlights 8ynw is a 4 chain structure with sequence from Bacillus thuringiensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Poly((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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 8ynw, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image