Structural highlights
Publication Abstract from PubMed
The adenosine monoposphate-forming acyl-CoA synthetase enzymes catalyze a two-step reaction that involves the initial formation of an acyl adenylate that reacts in a second partial reaction to form a thioester between the acyl substrate and CoA. These enzymes utilize a Domain Alternation catalytic mechanism, whereby a approximately 110 residue C-terminal domain rotates by 140 degrees to form distinct catalytic conformations for the two partial reactions. The structure of an acetoacetyl-CoA synthetase (AacS) is presented that illustrates a novel aspect of this C-terminal domain. Specifically, several acetyl- and acetoacetyl-CoA synthetases contain a 30-residue extension on the C-terminus compared to other members of this family. Whereas residues from this extension are disordered in prior structures, the AacS structure shows that residues from this extension may interact with key catalytic residues from the N-terminal domain. Proteins 2014. (c) 2014 Wiley Periodicals, Inc.
The structure of S. lividans acetoacetyl-CoA synthetase shows a novel interaction between the C-terminal extension and the N-terminal domain.,Mitchell CA, Tucker AC, Escalante-Semerena JC, Gulick AM Proteins. 2014 Dec 9. doi: 10.1002/prot.24738. PMID:25488501[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mitchell CA, Tucker AC, Escalante-Semerena JC, Gulick AM. The structure of S. lividans acetoacetyl-CoA synthetase shows a novel interaction between the C-terminal extension and the N-terminal domain. Proteins. 2014 Dec 9. doi: 10.1002/prot.24738. PMID:25488501 doi:http://dx.doi.org/10.1002/prot.24738
