Crystal Structure of TDP-Fucosamine Acetyltransferase (WecD) from
            <i>Escherichia coli</i>
            , an Enzyme Required for Enterobacterial Common Antigen Synthesis

Hung, Ming-Ni; Rangarajan, Erumbi S.; Munger, C.; Nadeau, Guy; Sulea, Traian; Matte, Allan

doi:10.1128/jb.00306-06

Cited by 27 publications

(41 citation statements)

References 86 publications

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“…The model organisms E. coli and S. enterica encode ϳ26 GNAT homologues, only half of which have known or predicted functions ( Table 2). These GNATs target primary amines (80,81), including the N termini of proteins (82,83), aminoglycoside antibiotics (63), polyamines (84), a nucleotide sugar (85), glutamate (86), toxic aminoacyl nucleotides (87), and transfer RNAs (88). Three GNAT enzymes, RimI, RimJ, and RimL, acetylate the ␣-amine group at the N terminus of the ribosomal proteins S18, S5, and L12, respectively (89,90).…”

Section: Bacterial Gcn5-related N-acyltransferasesmentioning

confidence: 99%

Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress

Hentchel

Escalante‐Semerena

2015

Microbiol Mol Biol Rev

163

175

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SUMMARY Acylation of biomolecules (e.g., proteins and small molecules) is a process that occurs in cells of all domains of life and has emerged as a critical mechanism for the control of many aspects of cellular physiology, including chromatin maintenance, transcriptional regulation, primary metabolism, cell structure, and likely other cellular processes. Although this review focuses on the use of acetyl moieties to modify a protein or small molecule, it is clear that cells can use many weak organic acids (e.g., short-, medium-, and long-chain mono- and dicarboxylic aliphatics and aromatics) to modify a large suite of targets. Acetylation of biomolecules has been studied for decades within the context of histone-dependent regulation of gene expression and antibiotic resistance. It was not until the early 2000s that the connection between metabolism, physiology, and protein acetylation was reported. This was the first instance of a metabolic enzyme (acetyl coenzyme A [acetyl-CoA] synthetase) whose activity was controlled by acetylation via a regulatory system responsive to physiological cues. The above-mentioned system was comprised of an acyltransferase and a partner deacylase. Given the reversibility of the acylation process, this system is also referred to as r eversible l ysine a cylation (RLA). A wealth of information has been obtained since the discovery of RLA in prokaryotes, and we are just beginning to visualize the extent of the impact that this regulatory system has on cell function.

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Section: Bacterial Gcn5-related N-acyltransferasesmentioning

confidence: 99%

Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress

Hentchel

Escalante‐Semerena

2015

Microbiol Mol Biol Rev

163

175

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“…The current LβH family members include: a bifunctional UDP- N -acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N -acetyltransferase (EC 2.3.1.157) GlmU from Escherichia coli, Mycobacterium tuberculosis and Yersinia pestis 73, 74, 80, 84 ; QdtC (responsible for N -acetylation of dTDP-Quip3N in Thermoanaerobacterium thermosaccharolyticum ) 169 ; PglD (responsible for N -acetylation of UDP-QuiNAc4N in Campylobacter jejuni ) 170, 171 ; WlbB (EC 2.3.1.B6, an enzyme that catalyzes N -acetylation of UDP-GlcNAcNA in Bordetella petrii ) 172 ; and the N -acyltransferase AntD (which catalyzes the acylation of the C4 amino group of dTDP-4-amino-4,6-dideoxyglucose using 3-hydroxy-3-methylbutyryl-CoA in Bacillus cereus en route to dTDP-D-Antrose 173 . The sole GNAT example from NDP-sugar biosynthesis reported to date is the dTDP-fucosamine acetyltransferase WecD from Escherichia coli 174 .…”

Section: Additional Sugar Modificationmentioning

confidence: 99%

“…The loop between α4 and α5 is longer in WecD than in other GNAT proteins and affects the size and shape of the substrate-binding site 174 . The NDP-sugar pyrophosphate forms hydrogen bonds to the backbone amide NH groups of G172 and G174 and to the side chain of R207.…”

Section: Additional Sugar Modificationmentioning

confidence: 99%

The structural biology of enzymes involved in natural product glycosylation

2012

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The glycosylation of microbial natural products often dramatically influences the biological and/or pharmacological activities of the parental metabolite. Over the past decade, crystal structures of several enzymes involved in the biosynthesis and attachment of novel sugars found appended to natural products have emerged. In many cases, these studies have paved the way to a better understanding of the corresponding enzyme mechanism of action and have served as a starting point for engineering variant enzymes to facilitate to production of differentially-glycosylated natural products. This review specifically summarizes the structural studies of bacterial enzymes involved in biosynthesis of novel sugar nucleotides.

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“…There are many reports of homodimeric glycosyltransferases (6,13,24,29). The dimeric structures have increased thermostability (27).…”

Section: Vol 84 2010 Virus-encoded Putative Glycosyltransferase 12269mentioning

confidence: 99%

Crystal Structure of a Virus-Encoded Putative Glycosyltransferase

Xiang

Baxa

Zhang

et al. 2010

J Virol

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The chloroviruses (family Phycodnaviridae), unlike most viruses, encode some, if not most, of the enzymes involved in the glycosylation of their structural proteins. Annotation of the gene product B736L from chlorovirus NY-2A suggests that it is a glycosyltransferase. The structure of the recombinantly expressed B736L protein was determined by X-ray crystallography to 2.3-Å resolution, and the protein was shown to have two nucleotide-binding folds like other glycosyltransferase type B enzymes. This is the second structure of a chlorovirus-encoded glycosyltransferase and the first structure of a chlorovirus type B enzyme to be determined. B736L is a retaining enzyme and belongs to glycosyltransferase family 4. The donor substrate was identified as GDP-mannose by isothermal titration calorimetry and was shown to bind into the cleft between the two domains in the protein. The active form of the enzyme is probably a dimer in which the active centers are separated by about 40 Å.

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Crystal Structure of TDP-Fucosamine Acetyltransferase (WecD) from Escherichia coli , an Enzyme Required for Enterobacterial Common Antigen Synthesis

Cited by 27 publications

References 86 publications

Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress

Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress

The structural biology of enzymes involved in natural product glycosylation

Crystal Structure of a Virus-Encoded Putative Glycosyltransferase

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