4KGB

Structure of succinyl-CoA: 3-ketoacid CoA transferase from Drosophila melanogaster

Summary for 4KGB

• Entry DOI: 10.2210/pdb4kgb/pdb
• Descriptor: Succinyl-CoA:3-ketoacid-coenzyme A transferase, SULFATE ION (3 entities in total)
• Functional Keywords: protein fold, ketone body catabolic process, transferase
• Biological source: Drosophila melanogaster (Fruit fly)
• Total number of polymer chains: 2
• Total formula weight: 103532.98

Authors

Wang, Y.C.,Shi, Z.B.,Zhang, M. (deposition date: 2013-04-29, release date: 2013-10-23, Last modification date: 2023-11-08)

Primary citation

Zhang, M.,Xu, H.Y.,Wang, Y.C.,Shi, Z.B.,Zhang, N.N.
Structure of succinyl-CoA:3-ketoacid CoA transferase from Drosophila melanogaster.
Acta Crystallogr.,Sect.F, 69:1089-1093, 2013

PubMed Abstract: Succinyl-CoA:3-ketoacid CoA transferase (SCOT) plays a crucial role in ketone-body metabolism. SCOT from Drosophila melanogaster (DmSCOT) was purified and crystallized. The crystal structure of DmSCOT was determined at 2.64 Å resolution and belonged to space group P212121, with unit-cell parameters a=76.638, b=101.921, c=122.457 Å, α=β=γ=90°. Sequence alignment and structural analysis identified DmSCOT as a class I CoA transferase. Compared with Acetobacter aceti succinyl-CoA:acetate CoA transferase, DmSCOT has a different substrate-binding pocket, which may explain the difference in their substrate specificities.

PubMed: 24100554
DOI: 10.1107/S1744309113024986

Experimental method

X-RAY DIFFRACTION (2.64 Å)