9knj

Crystal structure of glycerol-bound full-length PHA synthase (PhaC) from Aeromonas caviae

spinqualitylabelsall models 9knj, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9knj is a 3 chain structure with sequence from Aeromonas caviae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O32471_AERCA Publication Abstract from PubMed Polyhydroxyalkanoate (PHA) is a biodegradable polyester that can serve as a promising alternative to petrochemical plastics, which present a serious source of pollution. PHA synthase (PhaC) is a key enzyme responsible for producing a wide variety of PHAs in microorganisms. Here, we present crystal structures of full-length PhaC from Aeromonas caviae, a high-performance PhaC employed for industrial use. The structure reveals an N-terminal helical domain that mediates head-to-head dimerization and stabilizes the C-terminal alpha/beta catalytic domain to form a tunnel that connects the catalytic center embedded inside the protein to the protein surface. We showed that this tunnel is a putative egress tunnel for the product PHA chain. Our results establish a fundamental understanding of the PhaC machinery that should lead to improvement of this enzyme in industrial applications. Structures of Polyhydroxyalkanoate Synthase PhaC from Aeromonas caviae, Producing Biodegradable Plastics.,Chek MF, Kim SY, Mori T, Matsumoto K, Sato S, Hakoshima T Angew Chem Int Ed Engl. 2025 Apr 25:e202504626. doi: 10.1002/anie.202504626. PMID:40276819 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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