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4o9c

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Crystal structure of Beta-ketothiolase (PhaA) from Ralstonia eutropha H16Crystal structure of Beta-ketothiolase (PhaA) from Ralstonia eutropha H16

Structural highlights

4o9c is a 8 chain structure with sequence from Cupriavidus necator H16. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

THIL_CUPNH Catalyzes the condensation of two acetyl-coA units to form acetoacetyl-CoA. Is involved in the biosynthesis of polyhydroxybutyrate (PHB), which is accumulated as an intracellular energy reserve material when cells grow under conditions of nutrient limitation. Also catalyzes the reverse reaction, i.e. the cleavage of acetoacetyl-CoA, and is therefore also involved in the reutilization of PHB.[1] [2] [3]

See Also

References

  1. ↑ Peoples OP, Sinskey AJ. Poly-beta-hydroxybutyrate biosynthesis in Alcaligenes eutrophus H16. Characterization of the genes encoding beta-ketothiolase and acetoacetyl-CoA reductase. J Biol Chem. 1989 Sep 15;264(26):15293-7. PMID:2670935
  2. ↑ Peoples OP, Sinskey AJ. Poly-beta-hydroxybutyrate (PHB) biosynthesis in Alcaligenes eutrophus H16. Identification and characterization of the PHB polymerase gene (phbC). J Biol Chem. 1989 Sep 15;264(26):15298-303. PMID:2670936
  3. ↑ Oeding V, Schlegel HG. Beta-ketothiolase from Hydrogenomonas eutropha H16 and its significance in the regulation of poly-beta-hydroxybutyrate metabolism. Biochem J. 1973 May;134(1):239-48. PMID:4198758

4o9c, resolution 2.00Å

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