5HZ2
Crystal structure of PhaC1 from Ralstonia eutropha
Summary for 5HZ2
| Entry DOI | 10.2210/pdb5hz2/pdb |
| Descriptor | Poly-beta-hydroxybutyrate polymerase, GLYCEROL, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | transferase |
| Biological source | Cupriavidus necator |
| Cellular location | Cytoplasm: P23608 |
| Total number of polymer chains | 1 |
| Total formula weight | 44507.02 |
| Authors | Kim, J.,Kim, K.-J. (deposition date: 2016-02-02, release date: 2016-12-07, Last modification date: 2017-04-05) |
| Primary citation | Kim, J.,Kim, Y.J.,Choi, S.Y.,Lee, S.Y.,Kim, K.J. Crystal structure of Ralstonia eutropha polyhydroxyalkanoate synthase C-terminal domain and reaction mechanisms. Biotechnol J, 12:-, 2017 Cited by PubMed Abstract: Polyhydroxyalkanoates (PHAs) are natural polyesters synthesized by numerous microorganisms as energy and reducing power storage materials, and have attracted much attention as substitutes for petroleum-based plastics. Here, we report the first crystal structure of Ralstonia eutropha PHA synthase at 1.8 Å resolution and structure-based mechanisms for PHA polymerization. RePhaC1 contains two distinct domains, the N-terminal (RePhaC1 ) and C-terminal domains (RePhaC1 ), and exists as a dimer. RePhaC1 catalyzes polymerization via non-processive ping-pong mechanism using a Cys-His-Asp catalytic triad. Molecular docking simulation of 3-hydroxybutyryl-CoA to the active site of RePhaC1 reveals residues involved in the formation of 3-hydroxybutyryl-CoA binding pocket and substrate binding tunnel. Comparative analysis with other polymerases elucidates how different classes of PHA synthases show different substrate specificities. Furthermore, we attempted structure-based protein engineering and developed a RePhaC1 mutant with enhanced PHA synthase activity. PubMed: 27808482DOI: 10.1002/biot.201600648 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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