1ry2

Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMPCrystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP

Structural highlights

1ry2 is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ACS1_YEAST Catalyzes the production of acetyl-CoA. Provides the acetyl-CoA source for histone acetylation in the nucleus. "Aerobic" isozyme of acetyl-coenzyme A synthetase, which supports growth on nonfermentable carbon sources such as glycerol and ethanol. May be required for assimilation of ethanol and acetate.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Acetyl-coenzyme A synthetase (ACS) belongs to the family of AMP-forming enzymes that also includes acyl-CoA synthetases, firefly luciferase, and nonribosomal peptide synthetases. ACS catalyzes the two-step activation of acetate to acetyl-CoA: formation of an acetyl-AMP intermediate from acetate and ATP and the transfer of the acetyl group to CoA. In mammals, the acetyl-CoA product is used for biosynthesis of long chain fatty acids as well as energy production. We have determined the crystal structure of yeast ACS in a binary complex with AMP at 2.3 A resolution. The structure contains a large, N-terminal domain and a small, C-terminal domain. AMP is bound at the interface between the two domains. This structure represents a new conformation for the ACS enzyme, which may be competent for catalyzing the first step of the reaction. A Lys residue that is critical for this step is located in the active site. A rotation of 140 degrees in the small domain is needed for the binding of CoA and the catalysis of the second step. In contrast to the monomeric bacterial enzyme, yeast ACS is a stable trimer.

Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP.,Jogl G, Tong L Biochemistry. 2004 Feb 17;43(6):1425-31. PMID:14769018^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ van den Berg MA, de Jong-Gubbels P, Kortland CJ, van Dijken JP, Pronk JT, Steensma HY. The two acetyl-coenzyme A synthetases of Saccharomyces cerevisiae differ with respect to kinetic properties and transcriptional regulation. J Biol Chem. 1996 Nov 15;271(46):28953-9. PMID:8910545
↑ Takahashi H, McCaffery JM, Irizarry RA, Boeke JD. Nucleocytosolic acetyl-coenzyme a synthetase is required for histone acetylation and global transcription. Mol Cell. 2006 Jul 21;23(2):207-17. PMID:16857587 doi:http://dx.doi.org/10.1016/j.molcel.2006.05.040
↑ 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

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OCA

[1] van den Berg MA, de Jong-Gubbels P, Kortland CJ, van Dijken JP, Pronk JT, Steensma HY. The two acetyl-coenzyme A synthetases of Saccharomyces cerevisiae differ with respect to kinetic properties and transcriptional regulation. J Biol Chem. 1996 Nov 15;271(46):28953-9. PMID:8910545

[2] Takahashi H, McCaffery JM, Irizarry RA, Boeke JD. Nucleocytosolic acetyl-coenzyme a synthetase is required for histone acetylation and global transcription. Mol Cell. 2006 Jul 21;23(2):207-17. PMID:16857587 doi:http://dx.doi.org/10.1016/j.molcel.2006.05.040

[3] 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

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