Structural highlights
Function
[V1Q8H8_SALET] Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.[HAMAP-Rule:MF_01123] Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis.[HAMAP-Rule:MF_01123]
Publication Abstract from PubMed
Reversible lysine acetylation by protein acetyltransferases is a conserved regulatory mechanism that controls diverse cellular pathways. Gcn5-related N-acetyltransferases (GNATs), named after their founding member, are found in all domains of life. GNATs are known for their role as histone acetyltransferases, but non-histone bacterial protein acetytransferases have been identified. Only structures of GNAT complexes with short histone peptide substrates are available in databases. Given the biological importance of this modification and the abundance of lysine in polypeptides, how specificity is attained for larger protein substrates is central to understanding acetyl-lysine regulated networks. Here we report the structure of a GNAT in complex with a globular protein substrate solved to 1.9 Angstrom. GNAT binds the protein substrate with extensive surface interactions distinct from those reported for GNAT-peptide complexes. Our data reveal determinants needed for the recognition of a protein substrate and provide insight into the specificity of GNATs.
Insights Into the Specificity of Lysine Acetyltransferases.,Tucker AC, Taylor KC, Rank KC, Rayment I, Escalante-Semerena JC J Biol Chem. 2014 Nov 7. pii: jbc.M114.613901. PMID:25381442[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tucker AC, Taylor KC, Rank KC, Rayment I, Escalante-Semerena JC. Insights Into the Specificity of Lysine Acetyltransferases. J Biol Chem. 2014 Nov 7. pii: jbc.M114.613901. PMID:25381442 doi:http://dx.doi.org/10.1074/jbc.M114.613901
