4wd1

Acetoacetyl-CoA Synthetase from Streptomyces lividans

spinqualitylabelsall models 4wd1, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4wd1 is a 1 chain structure with sequence from Streptomyces lividans TK24. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.903Å Ligands: CA, EDO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D6EQU8_STRLI 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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