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Crystal structure of thermostable alkylsulfatase SdsAP from Pseudomonas sp. S9

A novel alkylsulfatase from bacterium Pseudomonas sp. S9 (SdsAP) was identified as a thermostable alkylsulfatases (type III), which could hydrolyze the primary alkyl sulfate such as sodium dodecyl sulfate (SDS). Thus, it has a potential application of SDS biodegradation. The crystal structure of Sds...

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Autores principales: Sun, Lifang, Chen, Pu, Su, Yintao, Cai, Zhixiong, Ruan, Lingwei, Xu, Xun, Wu, Yunkun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5426288/
https://www.ncbi.nlm.nih.gov/pubmed/28442601
http://dx.doi.org/10.1042/BSR20170001
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author Sun, Lifang
Chen, Pu
Su, Yintao
Cai, Zhixiong
Ruan, Lingwei
Xu, Xun
Wu, Yunkun
author_facet Sun, Lifang
Chen, Pu
Su, Yintao
Cai, Zhixiong
Ruan, Lingwei
Xu, Xun
Wu, Yunkun
author_sort Sun, Lifang
collection PubMed
description A novel alkylsulfatase from bacterium Pseudomonas sp. S9 (SdsAP) was identified as a thermostable alkylsulfatases (type III), which could hydrolyze the primary alkyl sulfate such as sodium dodecyl sulfate (SDS). Thus, it has a potential application of SDS biodegradation. The crystal structure of SdsAP has been solved to a resolution of 1.76 Å and reveals that SdsAP contains the characteristic metallo-β-lactamase-like fold domain, dimerization domain, and C-terminal sterol carrier protein type 2 (SCP-2)-like fold domain. Kinetic characterization of SdsAP to SDS by isothermal titration calorimetry (ITC) and enzymatic activity assays of constructed mutants demonstrate that Y246 and G263 are important residues for its preference for the hydrolysis of ‘primary alkyl’ chains, confirming that SdsAP is a primary alkylsulfatase.
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spelling pubmed-54262882017-05-24 Crystal structure of thermostable alkylsulfatase SdsAP from Pseudomonas sp. S9 Sun, Lifang Chen, Pu Su, Yintao Cai, Zhixiong Ruan, Lingwei Xu, Xun Wu, Yunkun Biosci Rep Research Articles A novel alkylsulfatase from bacterium Pseudomonas sp. S9 (SdsAP) was identified as a thermostable alkylsulfatases (type III), which could hydrolyze the primary alkyl sulfate such as sodium dodecyl sulfate (SDS). Thus, it has a potential application of SDS biodegradation. The crystal structure of SdsAP has been solved to a resolution of 1.76 Å and reveals that SdsAP contains the characteristic metallo-β-lactamase-like fold domain, dimerization domain, and C-terminal sterol carrier protein type 2 (SCP-2)-like fold domain. Kinetic characterization of SdsAP to SDS by isothermal titration calorimetry (ITC) and enzymatic activity assays of constructed mutants demonstrate that Y246 and G263 are important residues for its preference for the hydrolysis of ‘primary alkyl’ chains, confirming that SdsAP is a primary alkylsulfatase. Portland Press Ltd. 2017-05-11 /pmc/articles/PMC5426288/ /pubmed/28442601 http://dx.doi.org/10.1042/BSR20170001 Text en © 2017 The Author(s). http://creativecommons.org/licenses/by/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (http://creativecommons.org/licenses/by/4.0/) .
spellingShingle Research Articles
Sun, Lifang
Chen, Pu
Su, Yintao
Cai, Zhixiong
Ruan, Lingwei
Xu, Xun
Wu, Yunkun
Crystal structure of thermostable alkylsulfatase SdsAP from Pseudomonas sp. S9
title Crystal structure of thermostable alkylsulfatase SdsAP from Pseudomonas sp. S9
title_full Crystal structure of thermostable alkylsulfatase SdsAP from Pseudomonas sp. S9
title_fullStr Crystal structure of thermostable alkylsulfatase SdsAP from Pseudomonas sp. S9
title_full_unstemmed Crystal structure of thermostable alkylsulfatase SdsAP from Pseudomonas sp. S9
title_short Crystal structure of thermostable alkylsulfatase SdsAP from Pseudomonas sp. S9
title_sort crystal structure of thermostable alkylsulfatase sdsap from pseudomonas sp. s9
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5426288/
https://www.ncbi.nlm.nih.gov/pubmed/28442601
http://dx.doi.org/10.1042/BSR20170001
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