1PXT

THE 2.8 ANGSTROMS STRUCTURE OF PEROXISOMAL 3-KETOACYL-COA THIOLASE OF SACCHAROMYCES CEREVISIAE: A FIVE LAYERED A-B-A-B-A STRUCTURE, CONSTRUCTED FROM TWO CORE DOMAINS OF IDENTICAL TOPOLOGY

Summary for 1PXT

• Entry DOI: 10.2210/pdb1pxt/pdb
• Descriptor: PEROXISOMAL 3-KETOACYL-COA THIOLASE (1 entity in total)
• Functional Keywords: thiolase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Peroxisome: P27796
• Total number of polymer chains: 2
• Total formula weight: 83491.43

Authors

Mathieu, M.,Wierenga, R.K. (deposition date: 1994-07-04, release date: 1994-08-31, Last modification date: 2024-02-14)

Primary citation

Mathieu, M.,Zeelen, J.P.,Pauptit, R.A.,Erdmann, R.,Kunau, W.H.,Wierenga, R.K.
The 2.8 A crystal structure of peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: a five-layered alpha beta alpha beta alpha structure constructed from two core domains of identical topology.
Structure, 2:797-808, 1994

PubMed Abstract: The peroxisomal enzyme 3-ketoacyl-coenzyme A thiolase of the yeast Saccharomyces cerevisiae is a homodimer with 417 residues per subunit. It is synthesized in the cytosol and subsequently imported into the peroxisome where it catalyzes the last step of the beta-oxidation pathway. We have determined the structure of this thiolase in order to study the reaction mechanism, quaternary associations and intracellular targeting of thiolases generally, and to understand the structural basis of genetic disorders associated with human thiolases.

PubMed: 7812714
DOI: 10.1016/S0969-2126(94)00081-6

Experimental method

X-RAY DIFFRACTION (2.8 Å)