1QFL

BIOSYNTHETIC THIOLASE FROM ZOOGLOEA RAMIGERA IN COMPLEX WITH A REACTION INTERMEDIATE.

Summary for 1QFL

• Entry DOI: 10.2210/pdb1qfl/pdb
• Descriptor: PROTEIN (ACETOACETYL-COA THIOLASE), SULFATE ION, COENZYME A, ... (4 entities in total)
• Functional Keywords: thiolase, coa, tetramerization motif, covalent intermediate, acetyl-cysteine, transferase
• Biological source: Zoogloea ramigera
• Cellular location: Cytoplasm: P07097
• Total number of polymer chains: 4
• Total formula weight: 164838.31

Authors

Modis, Y.,Wierenga, R.K. (deposition date: 1999-04-12, release date: 2000-04-19, Last modification date: 2024-10-30)

Primary citation

Modis, Y.,Wierenga, R.K.
A biosynthetic thiolase in complex with a reaction intermediate: the crystal structure provides new insights into the catalytic mechanism.
Structure Fold.Des., 7:1279-1290, 1999

PubMed Abstract: Thiolases are ubiquitous and form a large family of dimeric or tetrameric enzymes with a conserved, five-layered alphabetaalphabetaalpha catalytic domain. Thiolases can function either degradatively, in the beta-oxidation pathway of fatty acids, or biosynthetically. Biosynthetic thiolases catalyze the biological Claisen condensation of two molecules of acetyl-CoA to form acetoacetyl-CoA. This is one of the fundamental categories of carbon skeletal assembly patterns in biological systems and is the first step in a wide range of biosynthetic pathways, including those that generate cholesterol, steroid hormones, and various energy-storage molecules.

PubMed: 10545327
DOI: 10.1016/S0969-2126(00)80061-1

Experimental method

X-RAY DIFFRACTION (1.92 Å)