Structure determination of BA0150, a putative polysaccharide deacetylase from <i>Bacillus anthracis</i>

Strunk, Robert J.; Piemonte, Katrina M.; Petersen, Natasha M.; Koutsioulis, Dimitris; Bouriotis, Vassilis; Perry, Kay; Cole, Kathryn

doi:10.1107/s2053230x13034262

Cited by 12 publications

(11 citation statements)

References 20 publications

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“…The structures of CE4 enzymes from various bacterial species have been determined, including PG deacetylases from Streptococcus pneumoniae ( 16 ) and Bacillus subtilis ( 17 ), acetylxylan esterases from Clostridium thermocellum and Streptomyces lividans ( 18 ), poly-β-1,6- N -acetyl- d -glucosamine deacetylase from Escherichia coli ( 19 ) and Staphylococcus epidermidis ( 20 ), and putative PDAs from B. anthracis ( 21 , 22 ), B. cereus ( 23 ), and Streptococcus mutans ( 24 ). CE4 enzymes contain a conserved NodB homology domain and adopt a (α/β) 8 barrel fold.…”

Section: Introductionmentioning

confidence: 99%

Two Putative Polysaccharide Deacetylases Are Required for Osmotic Stability and Cell Shape Maintenance in Bacillus anthracis

Arnaouteli

Giastas

Andreou

et al. 2015

Journal of Biological Chemistry

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Background: BA0330 and BA0331 are the only two lipoproteins among 11 known or putative polysaccharide deacetylases from Bacillus anthracis.Results: Both proteins lack deacetylase activity and are important for cell shape maintenance (BA0331) or high salt stress adaptation of the bacterium (BA0330).Conclusion: BA0330 and BA0331 stabilize the cell wall of B. anthracis.Significance: Understanding the mechanisms by which lipoproteins maintain cell wall integrity.

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Section: Introductionmentioning

confidence: 99%

Two Putative Polysaccharide Deacetylases Are Required for Osmotic Stability and Cell Shape Maintenance in Bacillus anthracis

Arnaouteli

Giastas

Andreou

et al. 2015

Journal of Biological Chemistry

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“…Bacillus anthracis BA0150 . Another putative Pda from B. anthracis ( Ba PdaB, BA0150) has been crystallized [ 72 ]. However, the crystal structure does not contain a catalytic metal ion, and the protein does not contain the conserved Asp–His–His metal-binding triad that is found in most of the CE4 enzymes, indicating that it is not a functional polysaccharide deacetylase.…”

Section: Ce4 Enzymes Active On Chitooligosaccharides and Their Submentioning

confidence: 99%

“…However, the crystal structure does not contain a catalytic metal ion, and the protein does not contain the conserved Asp–His–His metal-binding triad that is found in most of the CE4 enzymes, indicating that it is not a functional polysaccharide deacetylase. However, since it contains the conserved Asp and His catalytic residues, BA0150 may have some other hydrolytic activity [ 72 ].…”

Section: Ce4 Enzymes Active On Chitooligosaccharides and Their Submentioning

confidence: 99%

Substrate Recognition and Specificity of Chitin Deacetylases and Related Family 4 Carbohydrate Esterases

Aragunde

Biarnés

Planas

2018

IJMS

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Carbohydrate esterases family 4 (CE4 enzymes) includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases. Such biological functions make these enzymes attractive targets for drug design against pathogenic fungi and bacteria. On the other side, acetylxylan esterases deacetylate plant cell wall complex xylans to make them accessible to hydrolases, making them attractive biocatalysts for biomass utilization. CE4 family members are metal-dependent hydrolases. They are highly specific for their particular substrates, and show diverse modes of action, exhibiting either processive, multiple attack, or patterned deacetylation mechanisms. However, the determinants of substrate specificity remain poorly understood. Here, we review the current knowledge on the structure, activity, and specificity of CE4 enzymes, focusing on chitin deacetylases and related enzymes active on N-acetylglucosamine-containing oligo and polysaccharides.

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“…The three-dimensional structures of seven B. anthracis and B. cereus PDAs are now known [ 29 , 31 , 32 , 33 , 34 , 35 , 36 ]. On the structural level, CE4 members contain at least two distinct domains.…”

Section: Introductionmentioning

confidence: 99%

Structural and Evolutionary Insights within the Polysaccharide Deacetylase Gene Family of Bacillus anthracis and Bacillus cereus

Andreou

Giastas

Christoforides

et al. 2018

Genes

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Functional and folding constraints impose interdependence between interacting sites along the protein chain that are envisaged through protein sequence evolution. Studying the influence of structure in phylogenetic models requires detailed and reliable structural models. Polysaccharide deacetylases (PDAs), members of the carbohydrate esterase family 4, perform mainly metal-dependent deacetylation of O- or N-acetylated polysaccharides such as peptidoglycan, chitin and acetylxylan through a conserved catalytic core termed the NodB homology domain. Genomes of Bacillus anthracis and its relative Bacillus cereus contain multiple genes of putative or known PDAs. A comparison of the functional domains of the recently determined PDAs from B. anthracis and B. cereus and multiple amino acid and nucleotide sequence alignments and phylogenetic analysis performed on these closely related species showed that there were distinct differences in binding site formation, despite the high conservation on the protein sequence, the folding level and the active site assembly. This may indicate that, subject to biochemical verification, the binding site-forming sequence fragments are under functionally driven evolutionary pressure to accommodate and recognize distinct polysaccharide residues according to cell location, use, or environment. Finally, we discuss the suggestion of the paralogous nature of at least two genes of B. anthracis, ba0330 and ba0331, via specific differences in gene sequence, protein structure, selection pressure and available localization patterns. This study may contribute to understanding the mechanisms under which sequences evolve in their structures and how evolutionary processes enable structural variations.

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Structure determination of BA0150, a putative polysaccharide deacetylase from Bacillus anthracis

Cited by 12 publications

References 20 publications

Two Putative Polysaccharide Deacetylases Are Required for Osmotic Stability and Cell Shape Maintenance in Bacillus anthracis

Two Putative Polysaccharide Deacetylases Are Required for Osmotic Stability and Cell Shape Maintenance in Bacillus anthracis

Substrate Recognition and Specificity of Chitin Deacetylases and Related Family 4 Carbohydrate Esterases

Structural and Evolutionary Insights within the Polysaccharide Deacetylase Gene Family of Bacillus anthracis and Bacillus cereus

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