2WUA

Structure of the peroxisomal 3-ketoacyl-CoA thiolase from Sunflower

Summary for 2WUA

• Entry DOI: 10.2210/pdb2wua/pdb
• Related: 2WU9
• Descriptor: ACETOACETYL COA THIOLASE (2 entities in total)
• Functional Keywords: transferase, beta oxidation, plant lipid metabolism, acyltransferase, cysteine oxidation
• Biological source: HELIANTHUS ANNUUS (COMMON SUNFLOWER)
• Total number of polymer chains: 2
• Total formula weight: 92061.46

Authors

Pye, V.E.,Christensen, C.E.,Dyer, J.H.,Arent, S.,Henriksen, A. (deposition date: 2009-10-01, release date: 2010-05-12, Last modification date: 2023-12-20)

Primary citation

Pye, V.E.,Christensen, C.E.,Dyer, J.H.,Arent, S.,Henriksen, A.
Peroxisomal Plant 3-Ketoacyl-Coa Thiolases Structure and Activity are Regulated by a Sensitive Redox Switch
J.Biol.Chem., 285:24078-, 2010

PubMed Abstract: The breakdown of fatty acids, performed by the beta-oxidation cycle, is crucial for plant germination and sustainability. beta-Oxidation involves four enzymatic reactions. The final step, in which a two-carbon unit is cleaved from the fatty acid, is performed by a 3-ketoacyl-CoA thiolase (KAT). The shortened fatty acid may then pass through the cycle again (until reaching acetoacetyl-CoA) or be directed to a different cellular function. Crystal structures of KAT from Arabidopsis thaliana and Helianthus annuus have been solved to 1.5 and 1.8 A resolution, respectively. Their dimeric structures are very similar and exhibit a typical thiolase-like fold; dimer formation and active site conformation appear in an open, active, reduced state. Using an interdisciplinary approach, we confirmed the potential of plant KATs to be regulated by the redox environment in the peroxisome within a physiological range. In addition, co-immunoprecipitation studies suggest an interaction between KAT and the multifunctional protein that is responsible for the preceding two steps in beta-oxidation, which would allow a route for substrate channeling. We suggest a model for this complex based on the bacterial system.

PubMed: 20463027
DOI: 10.1074/JBC.M110.106013

Experimental method

X-RAY DIFFRACTION (1.8 Å)