4WD1
Acetoacetyl-CoA Synthetase from Streptomyces lividans
Summary for 4WD1
| Entry DOI | 10.2210/pdb4wd1/pdb |
| Descriptor | Acetoacetate-CoA ligase, 1,2-ETHANEDIOL, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | adenylate-forming enzyme, anl superfamily, ligase |
| Biological source | Streptomyces lividans TK24 |
| Total number of polymer chains | 1 |
| Total formula weight | 73777.00 |
| Authors | Gulick, A.M.,Mitchell, C.A. (deposition date: 2014-09-05, release date: 2015-01-28, Last modification date: 2023-09-27) |
| Primary citation | Mitchell, C.A.,Tucker, A.C.,Escalante-Semerena, J.C.,Gulick, A.M. The structure of S. lividans acetoacetyl-CoA synthetase shows a novel interaction between the C-terminal extension and the N-terminal domain. Proteins, 83:575-581, 2015 Cited by PubMed Abstract: 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. 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. PubMed: 25488501DOI: 10.1002/prot.24738 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.903 Å) |
Structure validation
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