5HZ2: Crystal Structure Of Phac1 From Ralstonia Eutropha

Citation:
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 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)
4
Poly-beta-hydroxybutyrate Polymerase
Molecule annotation
Chemicals (36 molecules)
1
8
2
28
* Click molecule labels to explore molecular sequence information.

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