Coker, Shu-Fen, Lloyd, Adrian J., Mitchell, Edward, Lewis, Gareth R., Coker, Alun R. and Shoolingin-Jordan, Peter M.. (2010) The high-resolution structure of pig heart succinyl-CoA:3-oxoacid coenzyme A transferase. Acta Crystallographica Section D Biological Crystallography, Vol.66 (No.7). pp. 797-805. ISSN 0907-4449

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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 angstrom 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.

Item Type:	Journal Article
Subjects:	Q Science > Q Science (General)
Divisions:	Faculty of Science > Life Sciences (2010- )
Journal or Publication Title:	Acta Crystallographica Section D Biological Crystallography
Publisher:	Wiley-Blackwell Publishing, Inc.
ISSN:	0907-4449
Official Date:	2010
Volume:	Vol.66
Number:	No.7
Number of Pages:	9
Page Range:	pp. 797-805
Identification Number:	10.1107/S0907444910018366
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access
URI:	http://wrap.warwick.ac.uk/id/eprint/42785

Data sourced from Thomson Reuters' Web of Knowledge

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