6AO7

Crystal Structure of a GNAT family acetyltransferase from Elizabethkingia anophelis with acetyl-CoA bound

Summary for 6AO7

• Entry DOI: 10.2210/pdb6ao7/pdb
• Descriptor: Acetyltransferase, ACETYL COENZYME *A, SULFATE ION, ... (4 entities in total)
• Functional Keywords: ssgcid, gnat family, structural genomics, seattle structural genomics center for infectious disease, transferase
• Biological source: Elizabethkingia anophelis
• Total number of polymer chains: 1
• Total formula weight: 19679.17

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2017-08-15, release date: 2017-08-30, Last modification date: 2023-10-04)

Primary citation

Shirmast, P.,Ghafoori, S.M.,Irwin, R.M.,Abendroth, J.,Mayclin, S.J.,Lorimer, D.D.,Edwards, T.E.,Forwood, J.K.
Structural characterization of a GNAT family acetyltransferase from Elizabethkingia anophelis bound to acetyl-CoA reveals a new dimeric interface.
Sci Rep, 11:1274-1274, 2021

PubMed Abstract: General control non-repressible 5 (GCN5)-related N-acetyltransferases (GNATs) catalyse the acetylation of a diverse range of substrates, thereby orchestrating a variety of biological processes within prokaryotes and eukaryotes. GNAT enzymes can catalyze the transfer of an acetyl group from acetyl coenzyme A to substrates such as aminoglycoside antibiotics, amino acids, polyamines, peptides, vitamins, catecholamines, and large macromolecules including proteins. Although GNATs generally exhibit low to moderate sequence identity, they share a conserved catalytic fold and conserved structural motifs. In this current study we characterize the high-resolution X-ray crystallographic structure of a GNAT enzyme bound with acetyl-CoA from Elizabethkingia anophelis, an important multi-drug resistant bacterium. The tertiary structure is comprised of six α-helices and nine β-strands, and is similar with other GNATs. We identify a new and uncharacterized GNAT dimer interface, which is conserved in at least two other unpublished GNAT structures. This suggests that GNAT enzymes can form at least five different types of dimers, in addition to a range of other oligomers including trimer, tetramer, hexamer, and dodecamer assemblies. The high-resolution structure presented in this study is suitable for future in-silico docking and structure-activity relationship studies.

PubMed: 33446675
DOI: 10.1038/s41598-020-79649-5

Experimental method

X-RAY DIFFRACTION (1.85 Å)