Gcn5-related n-acetyltransferase gnat
To determine the crystallographic structure of an uncharacterized GNAT from E. anophelis and allow the identification of key motifs and structural hallmarks common to GNAT family members, we first cloned the gene and recombinantly expressed the protein as a 6-His fusion (see “Materials and methods”). Following … See more Our structure contained a well-ordered acetyl-CoA molecule bound in the active site (Fig. 3AB). The interface between acetyl-CoA buries 593 Å2 of surface area and mediated by 10 hydrogen bonds. Key residues involved in … See more GNATs adopt a wide variety of assemblies, ranging from monomers, dimers, trimers, tetramers, hexamers, and dodecameric (double … See more WebGNAT, PS51186; Gcn5-related N-acetyltransferase (GNAT) domain profile (MATRIX) Sequences in UniProtKB/Swiss-Prot known to belong to this class: 721. detected by PS51186: 645 (true positives) undetected by PS51186: 76 (76 false negatives and 0 'partial') Other sequence(s) in UniProtKB/Swiss-Prot detected by PS51186: 1 false positive.
Gcn5-related n-acetyltransferase gnat
Did you know?
Web(1 of 1) PTHR13355//PTHR13355:SF12 - GLUCOSAMINE 6-PHOSPHATE N-ACETYLTRANSFERASE // GCN5-RELATED N-ACETYLTRANSFERASE (GNAT) FAMILY PROTEIN: C. reinhardtii v5.6: 5872 chromosome_10: 6192621-6198492: 1 Member Protein Name Organism Name ... WebAug 15, 2012 · Two domains are present in OsHAG702, namely a GCN5-related N-acetyltransferase (GNAT) domain (PS51186, residue range 168–315) and bromodomain (PF00439, 402–491). The 3D models of the GNAT domain and bromodomain analyzed with SWISS-MODEL Workspace [ 26 – 28 ] showed that high similarities existed among …
WebFeb 1, 2024 · Gcn5 serves as the defining member of the Gcn5-related N-acetyltransferase (GNAT) superfamily of proteins that display a common structural fold and catalytic mechanism involving the transfer of the acyl-group, primarily acetyl-, from CoA to an acceptor nucleophile. In the case of Gcn5, the target is the ε-amino group of lysine … WebApr 6, 2024 · GCN5-related N-acetyltransferase (GNAT) is a huge superfamily of proteins spanning the prokaryotic and eukaryotic domains of life. GNAT proteins usually transfer an acetyl group from acetyl-CoA to a wide variety of substrates ranging from aminoglycoside antibiotics to large macromolecules. Type II toxin–antitoxin (TA) modules are typically ...
WebGeneral control non-repressible 5 (GCN5)-related N-acetyltransferases (GNAT) catalyze the transfer of an acyl moiety from acyl coenzyme A (acyl-CoA) to a diverse group of substrates and are widely distributed in all … WebStructural Characterization of a Gcn5-Related N-Acetyltransferase from Staphylococcus aureus. The study provides the first high resolution structure of this GNAT enzyme from Staphyloccocus aureus, providing a strong platform for substrate and cofactor modelling, and structural/functional comparisons within this diverse enzyme superfamily.
WebThis review covers the three-dimensional structures of members of one of these superfamilies, now referred to in the literature as the GCN5-related N-acetyltransferases (GNAT), reflecting the importance of one functional category, the histone acetyltransferases. Despite the diversity of substrate specificities, members of the …
WebApr 12, 2024 · Enzymes in the Gcn5-related N-acetyltransferase (GNAT) superfamily are widespread and critically involved in multiple cellular processes ranging from antibiotic … the tigercat modular homeWebDec 23, 2024 · The enzymes of the GCN5-related N-acetyltransferase (GNAT) superfamily count more than 870 000 members through all kingdoms of life and share the same structural fold. GNAT enzymes transfer an acyl moiety from acyl coenzyme A to a wide range of substrates including aminoglycosides, serotonin, glucosamine-6 … the tiger centerWebSignal peptide: N GPI Anchor: N Predicted trans-membrane segments: 0 . Druggability Group : DG. Targets have been classified into druggability groups (DG) according to their druggability score in network driven prioritizations. DGs range from 1 to 5; the higher the group number, the higher the chance of the target to be druggable ... set priority real timeWebJan 27, 2016 · The GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes. Acetylation appears as a major regulatory post-translational modification and is as widespread as phosphorylation. N-Acetyltransferases transfer an acetyl group from … the tiger bridportWebSpermidine N-acetyltransferase (SpeG) prevents bacterial polyamine toxicity. The dodecameric three-dimensional structure of SpeG revealed an unknown polyamine allosteric site. SpeG acetylates spermidine/spermine using a … set private field c#WebHistone acetyltransferase 1 (HAT1) is a type B HAT that belongs to the Gcn5-related N-acetyltransferase (GNAT) family. The first function ascribed to HAT1 was catalysis of the rapid transfer of an acetyl group from acetyl coenzyme A exclusively onto the ε … the tiger chairWebJan 1, 2005 · The GNAT superfamily. The first members of what is now termed the GCN5-related N-acetyltransferase (GNAT) 1 superfamily were identified as aminoglycoside … set priority network adapter windows 10