5HZ2: Crystal Structure Of Phac1 From Ralstonia Eutropha

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 A resolution and structure-based mechanisms for PHA polymerization. RePhaC1 contains two distinct domains, the N-terminal (RePhaC1ND ) and C-terminal domains (RePhaC1CD ), and exists as a dimer. RePhaC1CD 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 RePhaC1CD 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.
PDB ID: 5HZ2Download
MMDB ID: 145435
PDB Deposition Date: 2016/2/2
Updated in MMDB: 2016/12
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 5HZ2: tetrameric; determined by author and by software (PISA)
Molecular Components in 5HZ2
Label Count Molecule
Proteins (4 molecules)
Poly-beta-hydroxybutyrate Polymerase
Molecule annotation
Chemicals (36 molecules)
* Click molecule labels to explore molecular sequence information.

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