Our analyses reveal many additional GNAT (GCN5-related N-acetyltransferase) superfamily members (Fig. 1), including the yeast Spt10p protein.NeuwaldAndrewF.LandsmanDavidTrends in biochemical sciencesNeuwald AF, Landsman D. GCN5-related histone N-acetyltransferases belong to a diverse superfamily that...
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 X-ray structure of a canonical GCN5-related N-acetyltransferase (GNAT), Serratia marcescens aminoglycoside 3-N-acetyltransferase, bound to coenzyme A (CoA) has been determined at 2.3 Å resolution. The single domain α/β protein resembles a cupped right hand wrapped around a cylinder and...
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
From structural and functional analysis, the C-terminal region ofRmNag was identified as a unique tandem array linking general control non-derepressible 5 (GCN5)-related N-acetyltransferase (GNAT), which displayed glucosamine N-acetyltransferase activity. Structural analysis of this glucosamine N-...
Gcn5‐related N‐acetyltransferaseproduct‐based transition‐state modelingradical‐mediated bisubstrateGcn5‐related N‐acetyltransferases (GNATs) are found in all kingdoms of life and catalyze important acyl transfer reactions in diverse cellular processes. While many 3D structures of GNATs have been ...
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 ...
Crystal structure of a GCN5-related N-acetyltransferase: Serratia marcescens aminoglycoside 3-N-acetyltransferase. Cell. 1998; 94:439-449. [PubMed: 9727487]Crystal structure of aGCN5-related N-acetyltransferase: Serratia marcescens aminoglycoside3-N-acetyltransferase. WOLF E,VASSILEV A,MAKINO Y, et ...
Our structural study reveals that bribT is a member of GCN5-related N-acetyltransferase (GNAT) superfamily and contains all the four conserved structural motifs that have been in other members of GNAT superfamily. The members of GNAT family transfers the acetyl group from acetyl coenzyme A (AcC...
(NAT) domain in the GCN5-relatedN-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 two putative, functionally distinct domains of Ngs1 are both required for Ngs1 ...