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Extracellular alpha/beta-hydrolase from Paenibacillus species shares structural and functional homology to tobacco salicylic acid binding protein 2
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Wilkinson, Rachael C., Rahmanpour, Rahman, Jamshidi, Shirin, Fülöp, Vilmos and Bugg, Timothy D. H. (2020) Extracellular alpha/beta-hydrolase from Paenibacillus species shares structural and functional homology to tobacco salicylic acid binding protein 2. Journal of Structural Biology, 210 (3). 107496. doi:10.1016/j.jsb.2020.107496 ISSN 1047-8477.
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WRAP-Extracellular-alphabeta-hydrolase-Paenibacillus-Salicylic-Bugg-2020.pdf - Accepted Version - Requires a PDF viewer. Available under License Creative Commons Attribution Non-commercial No Derivatives 4.0. Download (1329Kb) | Preview |
Official URL: https://doi.org/10.1016/j.jsb.2020.107496
Abstract
An alpha/ beta hydrolase annotated as a putative salicylate esterase within the genome of a species of Paenibacillus previously identified from differential and selective growth on Kraft lignin was structurally and functionally characterised. Feruloyl esterases are key to the degradation of lignin in several bacterial species and although this activity was investigated, no such activity was observed. The crystal structure of the Paenibacillus esterase, here denoted as PnbE, was determined at 1.32 Å resolution, showing high similarity to Nicotiana tabacum salicylic acid binding protein 2 from the protein database. Structural similarities between these two structures across the core domains and key catalytic residues were observed, with superposition of catalytic residues giving an RMSD of 0.5 Å across equivalent Cα atoms. Conversely, the cap domains of PnbE and Nicotiana tabacum SABP2 showed greater divergence with decreased flexibility in the PnbE cap structure. Activity of PnbE as a putative methyl salicylate esterase was supported with binding studies showing affinity for salicylic acid and functional studies showing methyl salicylate esterase activity. We hypothesise that this activity could enrich Paenibacillus sp. within the rhizosphere by increasing salicylic acid concentrations within the soil.
Item Type: | Journal Article | ||||||||
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) |
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Journal or Publication Title: | Journal of Structural Biology | ||||||||
Publisher: | Academic Press | ||||||||
ISSN: | 1047-8477 | ||||||||
Official Date: | 1 June 2020 | ||||||||
Dates: |
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Volume: | 210 | ||||||||
Number: | 3 | ||||||||
Article Number: | 107496 | ||||||||
DOI: | 10.1016/j.jsb.2020.107496 | ||||||||
Status: | Peer Reviewed | ||||||||
Publication Status: | Published | ||||||||
Access rights to Published version: | Restricted or Subscription Access | ||||||||
Date of first compliant deposit: | 25 March 2020 | ||||||||
Date of first compliant Open Access: | 26 March 2021 | ||||||||
RIOXX Funder/Project Grant: |
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