Open AccessStructure of succinyl‐CoA:3‐ketoacid CoA transferase from Drosophila melanogaster
Author(s) -
Zhang Min,
Xu HanYang,
Wang YiCui,
Shi ZhuBing,
Zhang NanNan
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113024986
Subject(s) - drosophila melanogaster , transferase , chemistry , biochemistry , enzyme , gene
Succinyl‐CoA:3‐ketoacid CoA transferase (SCOT) plays a crucial role in ketone‐body metabolism. SCOT from Drosophila melanogaster ( Dm SCOT) was purified and crystallized. The crystal structure of Dm SCOT was determined at 2.64 Å resolution and belonged to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 76.638, b = 101.921, c = 122.457 Å, α = β = γ = 90°. Sequence alignment and structural analysis identified Dm SCOT as a class I CoA transferase. Compared with Acetobacter aceti succinyl‐CoA:acetate CoA transferase, Dm SCOT has a different substrate‐binding pocket, which may explain the difference in their substrate specificities.