3K6M
Dynamic domains of Succinyl-CoA:3-ketoacid-coenzyme A transferase from pig heart.
Summary for 3K6M
| Entry DOI | 10.2210/pdb3k6m/pdb |
| Related | 1M3E 1O9L 1OOY 1OOZ 1OPE 2NRB |
| Descriptor | Succinyl-CoA:3-ketoacid-coenzyme A transferase 1, mitochondrial, CHLORIDE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | scot, coa transferase, dynamic domain, glycerol, mitochondrion, transferase, transit peptide |
| Biological source | Sus scrofa (pig) |
| Cellular location | Mitochondrion: Q29551 |
| Total number of polymer chains | 4 |
| Total formula weight | 209430.92 |
| Authors | Coker, S.,Lloyd, A.,Mitchell, E.,Lewis, G.R.,Shoolingin-Jordan, P.,Coker, A.R. (deposition date: 2009-10-09, release date: 2010-07-07, Last modification date: 2023-09-06) |
| Primary citation | Coker, S.F.,Lloyd, A.J.,Mitchell, E.,Lewis, G.R.,Coker, A.R.,Shoolingin-Jordan, P.M. The high-resolution structure of pig heart succinyl-CoA:3-oxoacid coenzyme A transferase. Acta Crystallogr.,Sect.D, 66:797-805, 2010 Cited by PubMed Abstract: The enzyme succinyl-CoA:3-oxoacid coenzyme A transferase (SCOT) participates in the metabolism of ketone bodies in extrahepatic tissues. It catalyses the transfer of coenzyme A (CoA) from succinyl-CoA to acetoacetate with a classical ping-pong mechanism. There is biochemical evidence that the enzyme undergoes conformational changes during the reaction, but no domain movements have been reported in the available crystal structures. Here, a structure of pig heart SCOT refined at 1.5 A resolution is presented, showing that one of the four enzyme subunits in the crystallographic asymmetric unit has a molecule of glycerol bound in the active site; the glycerol molecule is hydrogen bonded to the conserved catalytic glutamate residue and is likely to occupy the cosubstrate-binding site. The binding of glycerol is associated with a substantial relative movement (a 13 degrees rotation) of two previously undefined domains that close around the substrate-binding site. The binding orientation of one of the cosubstrates, acetoacetate, is suggested based on the glycerol binding and the possibility that this dynamic domain movement is of functional importance is discussed. PubMed: 20606260DOI: 10.1107/S0907444910018366 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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