Acetyl-CoA synthetase

From Proteopedia

Revision as of 12:11, 3 December 2015

spinqualitylabelsall models 2 monomers of acetyl-CoA synthetase complex with CoA and AMP (PDB code 2p2j) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Acetyl-CoA synthetase (ACS) catalyzes the ligation of acetate and CoA to form acetyl-CoA with the conversion of ATP to AMP and pyrophosphate. ACS is an ATP-dependent AMP-binding enzyme. Mg+2 is ACS cofactor. ACS participates in the pathway which fixes CO2 under anaerobic conditions. ACS acetylates the response regulator for flagellar movement and for chemotaxis - CheY. [1] Relevance Acetyl-CoA is used in aerobic respiration to produce energy and electron carriers and for lipid biosynthesis, in histone acetylation which is critical for DNA condensation to chromatin. Structural Highlights . . (2p2j).[2]

3D structures of acetyl-CoA synthetase

Updated on 03-December-2015

1pg3, 1pg4 – SeACS (mutant) + CoA + AMP – Salmonella enterica
2p20, 2p2m, 2p2q - StACS (mutant) + AMP – Salmonella typhimurium
2p2b, 2p2j - StACS (mutant) + CoA + AMP
2p2f - StACS + CoA + AMP
1ry2 – ACS + AMP - yeast
4u5y – ACS GNAT domain + SeACS C terminal (mutant) – Streptomyces lividans

References

1. ↑ Jogl G, Tong L. Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP. Biochemistry. 2004 Feb 17;43(6):1425-31. PMID:14769018 doi:10.1021/bi035911a
2. ↑ Reger AS, Carney JM, Gulick AM. Biochemical and crystallographic analysis of substrate binding and conformational changes in acetyl-CoA synthetase. Biochemistry. 2007 Jun 5;46(22):6536-46. Epub 2007 May 12. PMID:17497934 doi:http://dx.doi.org/10.1021/bi6026506