1POI

CRYSTAL STRUCTURE OF GLUTACONATE COENZYME A-TRANSFERASE FROM ACIDAMINOCOCCUS FERMENTANS TO 2.55 ANGSTOMS RESOLUTION

Summary for 1POI

• Entry DOI: 10.2210/pdb1poi/pdb
• Descriptor: GLUTACONATE COENZYME A-TRANSFERASE, COPPER (II) ION, ... (4 entities in total)
• Functional Keywords: transferase, coa, glutamate, protein fermentation
• Biological source: Acidaminococcus fermentans; More
• Cellular location: Cytoplasm: Q59111 Q59112
• Total number of polymer chains: 4
• Total formula weight: 127977.19

Authors

Jacob, U.,Mack, M.,Clausen, T.,Huber, R.,Buckel, W.,Messerschmidt, A. (deposition date: 1997-01-24, release date: 1998-03-18, Last modification date: 2024-02-14)

Primary citation

Jacob, U.,Mack, M.,Clausen, T.,Huber, R.,Buckel, W.,Messerschmidt, A.
Glutaconate CoA-transferase from Acidaminococcus fermentans: the crystal structure reveals homology with other CoA-transferases.
Structure, 5:415-426, 1997

PubMed Abstract: Coenzyme A-transferases are a family of enzymes with a diverse substrate specificity and subunit composition. Members of this group of enzymes are found in anaerobic fermenting bacteria, aerobic bacteria and in the mitochondria of humans and other mammals, but so far none have been crystallized. A defect in the human gene encoding succinyl-CoA: 3-oxoacid CoA-transferase causes a metabolic disease which leads to severe ketoacidosis, thus reflecting the importance of this family of enzymes. All CoA-transferases share a common mechanism in which the CoA moiety is transferred from a donor (e.g. acetyl CoA) to an acceptor, (R)-2-hydroxyglutarate, whereby acetate is formed. The transfer has been described by a ping-pong mechanism in which CoA is bound to the active-site residue of the enzyme as a covalent thiol ester intermediate. We describe here the crystal structure of glutaconate CoA-transferase (GCT) from the strictly anaerobic bacterium Acidaminococcus fermentans. This enzyme activates (R)-2-hydroxyglutarate to (R)-2-hydroxyglutaryl-CoA in the pathway of glutamate fermentation. We initiated this project to gain further insight into the function of this enzyme and the structural basis for the characteristics of CoA-transferases.

PubMed: 9083111
DOI: 10.1016/S0969-2126(97)00198-6

Experimental method

X-RAY DIFFRACTION (2.5 Å)