Reports that GCN5-related histone acetyltransferase (HAT) belong to a far more extensive superfamily of both known and putative N-acetyltransferases (NAT). Two regions of sequence similarity; Functional significance of the conserved residues in the two regions; Limited analysis employed in order to ...
Here, we present the 2.3 Å resolution X-ray structure of Serratia marcescens aminoglycoside-3-N-acetyltransferase (AAT) (Javier Teran et al. 1992) bound to CoA. Our work provides a structure for the canonical N-acetyltransferase fold common to all GCN5-related N-acetyltransferases. The α/...
The C-terminal region of Ngs1 has a weak homology to the N-Acyltransferase (NAT) domain in the GCN5-related N-acetyltransferase (GNAT) family31,32 (Fig. 2a). In front of the NAT domain lays a putative nuclear localization signal (NLS), predicted by cNLS Mapper33 (Fig. 2a). The ...
The C-terminal region of Ngs1 is essential for growth on GlcNAc and contains a weak sequence homology to the NAT domain of the GCN5-related N-acetyltransferase (GNAT) family31,32. GNAT members are known to share weak similarities by sequence alignment, but they all have a universally conserv...
We report the crystal structure of the yeast protein Hpa2 in complex with acetyl coenzyme A (AcCoA) at 2.4 A resolution and without cofactor at 2.9 A resolution. Hpa2 is a member of the Gcn5-related N-acetyltransferase (GNAT) superfamily, a family of enz
The protein is monomeric, with a fold that places it in the GCN5-related N-acetyltransferase (GNAT) family of acyltransferases. Features of the structure are an acyl-CoA binding site that is shared with other GNAT family members and an adjacent hydrophobic channel leading to the surface that ...
The Gcn5-related N-acetyltransferases contain one of the largest enzyme superfamilies in sequenced genomes. This yeast transcriptional regulator, Gcn5, was shown to have sequence homology with N-acetyltransferase.MichaelDepartment of Biochemistryde Carvalho...
Acetylating Polymyxin Antibiotics: Clues Toward Substrate Specificity of PA3944 Gcn5‐related N‐acetyltransferase of Unknown FunctionAlthough Gcn5-related N-acetyltransferases (GNATs) have been studied for several decades in the context of aminoglycoside resistance and histone acetylation, the majority of ...
1998 . Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Cell. 94(4):427–438.Dutnall RN, Tafrov ST, Sternglanz R, Ramakrishnan V. Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-...
Wybenga-Groot LE, Draker K, Wright GD, Berghuis AM (1999) Crystal struc- ture of an aminoglycoside 6#-N-acetyltransferase: defining the GCN5- related N-acetyltransferase superfamily fold. Structure 7: 497-507Wybenga-Groot LE , Draker K , Wright GD , Berghuis AM ( 1999 ) Crystal ...