The structure of S . lividans acetoacetyl-CoA synthetase shows a novel interaction between the C-terminal extension and the N-terminal domain
- Hauptman-Woodward Institute, Buffalo New York 14203; Department of Structural Biology, University at Buffalo, Buffalo New York 14203
- Department of Microbiology, University of Georgia, Athens Georgia 30602
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 ~110 residue C-terminal domain rotates by 140° to form distinct catalytic conformations for the two partial reactions. In this paper, 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. Finally, 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.
- Research Organization:
- Hauptman-Woodward Inst., Buffalo, NY (United States); Univ. at Buffalo, NY (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER)
- Grant/Contract Number:
- AC02-76SF00515; GM-068440; GM062203
- OSTI ID:
- 1343103
- Journal Information:
- Proteins, Vol. 83, Issue 3; ISSN 0887-3585
- Publisher:
- WileyCopyright Statement
- Country of Publication:
- United States
- Language:
- English
Web of Science
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