Functional Profiling and Crystal Structures of Isothiocyanate Hydrolases Found in Gut-Associated and Plant-Pathogenic Bacteria

van den Bosch, Tijs J. M.; Tan, Kemin; Joachimiak, Andrzej; Welte, Cornelia U.; Kivisaar, Maia

doi:10.1128/AEM.00478-18

Title: Functional Profiling and Crystal Structures of Isothiocyanate Hydrolases Found in Gut-Associated and Plant-Pathogenic Bacteria

Journal Article · 01 July 2018 · Applied and Environmental Microbiology

DOI: https://doi.org/10.1128/AEM.00478-18 · OSTI ID:1467602

van den Bosch, Tijs J. M. ^[1]; Tan, Kemin ^[2]; Joachimiak, Andrzej ^[2];

^[3]; Kivisaar, Maia ^[4]

Radboud Univ., Nijmegen (The Netherlands)
Argonne National Lab. (ANL), Lemont, IL (United States); Univ. of Chicago, Chicago, IL (United States)
Radboud Univ., Nijmegen (The Netherlands); Soehngen Institute for Anaerobic Microbiology, Nijmegen (The Netherlands)
Univ. of Tartu, Tartu (Estonia)

Isothiocyanates (ITCs) are produced by cruciferous plants to protect them against herbivores and infection by microbes. These compounds are of particular interest due to their antimicrobial and anticarcinogenic properties. The breakdown of ITCs in nature is catalyzed by isothiocyanate hydrolases (ITCases), a novel family within the metallo-β-lactamase (MBL)-fold superfamily of proteins. saxA genes that code for ITCases are particularly widespread in insect- and plant-associated bacteria. Enzymatic characterization of seven phylogenetically related but distinct ITCases revealed similar activities on six selected ITCs, suggesting that phylogenetic diversity does not determine the substrate specificity of ITCases. X-ray crystallography studies of two ITCases sharing 42% amino acid sequence identity revealed a highly conserved tertiary structure. Notable features of ITCases include a hydrophobic active site with two Zn²⁺ ions coordinating water/hydroxide and a flexible cap that is implicated in substrate recognition and covers the active site. Furthermore, this report reveals the function and structure of the previously uncharacterized family of isothiocyanate hydrolases within the otherwise relatively well-studied superfamily of metallo-β-lactamases.

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Research Organization:: Argonne National Lab. (ANL), Argonne, IL (United States)

Sponsoring Organization:: National Institutes of Health (NIH); Netherlands Organisation for Scientific Research (NWO); USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1467602

Journal Information:: Applied and Environmental Microbiology, Journal Name: Applied and Environmental Microbiology Journal Issue: 14 Vol. 84; ISSN 0099-2240

Publisher:: American Society for MicrobiologyCopyright Statement

Country of Publication:: United States

Language:: English

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59 BASIC BIOLOGICAL SCIENCES
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isothiocyanate hydrolase
metallo-β-lactamase superfamily
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Title: Functional Profiling and Crystal Structures of Isothiocyanate Hydrolases Found in Gut-Associated and Plant-Pathogenic Bacteria

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