Structural characterization of a Gcn5-related N-acetyltransferase from Staphylococcus aureus.

The Gcn5-related N-acetyltransferases (GNATs) are ubiquitously expressed in nature and perform a diverse range of cellular functions through the acetylation of small molecules and protein substrates. Using activated acetyl coenzyme A as a common acetyl donor, GNATs catalyse the transfer of an acetyl...

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Autores principales:	Parul Srivastava, Yogesh B Khandokar, Crystall M D Swarbrick, Noelia Roman, Zainab Himiari, Subir Sarker, Shane R Raidal, Jade K Forwood
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/89230eb841c74cfd951692340819ba54
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spelling	oai:doaj.org-article:89230eb841c74cfd951692340819ba542021-11-25T06:04:59ZStructural characterization of a Gcn5-related N-acetyltransferase from Staphylococcus aureus.1932-620310.1371/journal.pone.0102348https://doaj.org/article/89230eb841c74cfd951692340819ba542014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/25118709/?tool=EBIhttps://doaj.org/toc/1932-6203The Gcn5-related N-acetyltransferases (GNATs) are ubiquitously expressed in nature and perform a diverse range of cellular functions through the acetylation of small molecules and protein substrates. Using activated acetyl coenzyme A as a common acetyl donor, GNATs catalyse the transfer of an acetyl group to acceptor molecules including aminoglycoside antibiotics, glucosamine-6-phosphate, histones, serotonin and spermidine. There is often only very limited sequence conservation between members of the GNAT superfamily, in part, reflecting their capacity to bind a diverse array of substrates. In contrast, the secondary and tertiary structures are highly conserved, but then at the quaternary level there is further diversity, with GNATs shown to exist in monomeric, dimeric, or tetrameric states. Here we describe the X-ray crystallographic structure of a GNAT enzyme from Staphylococcus aureus with only low sequence identity to previously solved GNAT proteins. It contains many of the classical GNAT motifs, but lacks other hallmarks of the GNAT fold including the classic β-bulge splayed at the β-sheet interface. The protein is likely to be a dimer in solution based on analysis of the asymmetric unit within the crystal structure, homology with related GNAT family members, and size exclusion chromatography. The study provides the first high resolution structure of this enzyme, providing a strong platform for substrate and cofactor modelling, and structural/functional comparisons within this diverse enzyme superfamily.Parul SrivastavaYogesh B KhandokarCrystall M D SwarbrickNoelia RomanZainab HimiariSubir SarkerShane R RaidalJade K ForwoodPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 8, p e102348 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Parul Srivastava Yogesh B Khandokar Crystall M D Swarbrick Noelia Roman Zainab Himiari Subir Sarker Shane R Raidal Jade K Forwood Structural characterization of a Gcn5-related N-acetyltransferase from Staphylococcus aureus.
description	The Gcn5-related N-acetyltransferases (GNATs) are ubiquitously expressed in nature and perform a diverse range of cellular functions through the acetylation of small molecules and protein substrates. Using activated acetyl coenzyme A as a common acetyl donor, GNATs catalyse the transfer of an acetyl group to acceptor molecules including aminoglycoside antibiotics, glucosamine-6-phosphate, histones, serotonin and spermidine. There is often only very limited sequence conservation between members of the GNAT superfamily, in part, reflecting their capacity to bind a diverse array of substrates. In contrast, the secondary and tertiary structures are highly conserved, but then at the quaternary level there is further diversity, with GNATs shown to exist in monomeric, dimeric, or tetrameric states. Here we describe the X-ray crystallographic structure of a GNAT enzyme from Staphylococcus aureus with only low sequence identity to previously solved GNAT proteins. It contains many of the classical GNAT motifs, but lacks other hallmarks of the GNAT fold including the classic β-bulge splayed at the β-sheet interface. The protein is likely to be a dimer in solution based on analysis of the asymmetric unit within the crystal structure, homology with related GNAT family members, and size exclusion chromatography. The study provides the first high resolution structure of this enzyme, providing a strong platform for substrate and cofactor modelling, and structural/functional comparisons within this diverse enzyme superfamily.
format	article
author	Parul Srivastava Yogesh B Khandokar Crystall M D Swarbrick Noelia Roman Zainab Himiari Subir Sarker Shane R Raidal Jade K Forwood
author_facet	Parul Srivastava Yogesh B Khandokar Crystall M D Swarbrick Noelia Roman Zainab Himiari Subir Sarker Shane R Raidal Jade K Forwood
author_sort	Parul Srivastava
title	Structural characterization of a Gcn5-related N-acetyltransferase from Staphylococcus aureus.
title_short	Structural characterization of a Gcn5-related N-acetyltransferase from Staphylococcus aureus.
title_full	Structural characterization of a Gcn5-related N-acetyltransferase from Staphylococcus aureus.
title_fullStr	Structural characterization of a Gcn5-related N-acetyltransferase from Staphylococcus aureus.
title_full_unstemmed	Structural characterization of a Gcn5-related N-acetyltransferase from Staphylococcus aureus.
title_sort	structural characterization of a gcn5-related n-acetyltransferase from staphylococcus aureus.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/89230eb841c74cfd951692340819ba54
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Structural characterization of a Gcn5-related N-acetyltransferase from Staphylococcus aureus.

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