9KNL
Crystal structure of triethylene glycol-bound full-length PHA synthase (PhaC) from Aeromonas caviae
Summary for 9KNL
| Entry DOI | 10.2210/pdb9knl/pdb |
| Descriptor | PHA synthase, TRIETHYLENE GLYCOL (3 entities in total) |
| Functional Keywords | pha synthase, full-length phac, dimer, tunnel, catalytic triad, polyhydroxyalkanoates, biosynthetic protein |
| Biological source | Aeromonas caviae |
| Total number of polymer chains | 3 |
| Total formula weight | 199963.33 |
| Authors | |
| Primary citation | Chek, M.F.,Kim, S.Y.,Mori, T.,Matsumoto, K.,Sato, S.,Hakoshima, T. Structures of Polyhydroxyalkanoate Synthase PhaC from Aeromonas caviae, Producing Biodegradable Plastics. Angew.Chem.Int.Ed.Engl., :e202504626-e202504626, 2025 Cited by PubMed Abstract: 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 α/β 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. PubMed: 40276819DOI: 10.1002/anie.202504626 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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