In:
Biotechnology Journal, Wiley, Vol. 12, No. 1 ( 2017-01)
Kurzfassung:
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. In an accompanying paper, the authors reported the crystal structure of the C‐terminal domain of Ralstonia eutropha PHA synthase (PhaC1). Here, the authors report the 3D reconstructed model of full‐length of R. eutropha PhaC1 ( Re PhaC1 F ) by small angle X‐ray scattering (SAXS) analysis. The catalytic C‐terminal domain of Re PhaC1 ( Re PhaC1 CD ) dimer is located at the center of Re PhaC1 F , and the N‐terminal domain of Re PhaC1 ( Re PhaC1 ND ) is located opposite the dimerization subdomain of Re PhaC1 CD , indicating that Re PhaC1 ND is not directly involved in the enzyme catalysis. The localization studies using Re PhaC1 F , Re PhaC1 ND and Re PhaC1 CD revealed that Re PhaC1 ND plays important roles in PHA polymerization by localizing the enzyme to the PHA granules and stabilizing the growing PHA polymer near the active site of Re PhaC1 CD . The serial truncation study on Re PhaC1 ND suggested that the predicted five α‐helices (N‐α3 to N‐α7) are required for proper folding and granule binding function of Re PhaC1 ND . In addition, the authors also report the SAXS 3D reconstructed model of the Re PhaC1 F / Re PhaM ΔC complex ( Re PhaM ΔC , PAKKA motif‐truncated version of Re PhaM). Re PhaM forms a complex with Re PhaC1 by interacting with Re PhaC1 ND and activates Re PhaC1 by providing a more extensive surface area for interaction with the growing PHA polymer.
Materialart:
Online-Ressource
ISSN:
1860-6768
,
1860-7314
DOI:
10.1002/biot.201600649
Sprache:
Englisch
Verlag:
Wiley
Publikationsdatum:
2017
ZDB Id:
2214038-4
