Structural insight into a CE15 esterase from the marine bacterial metagenome
The family 15 carbohydrate esterase (CE15) MZ0003, which derives from a marine Arctic metagenome, has a broader substrate scope than other members of this family. Here we report the crystal structure of MZ0003, which reveals that residues comprising the catalytic triad differ from previously-charact...
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ftpubmed:oai:pubmedcentral.nih.gov:5722869 2023-05-15T15:07:05+02:00 Structural insight into a CE15 esterase from the marine bacterial metagenome De Santi, Concetta Gani, Osman ABSM Helland, Ronny Williamson, Adele 2017-12-08 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5722869/ http://www.ncbi.nlm.nih.gov/pubmed/29222424 https://doi.org/10.1038/s41598-017-17677-4 en eng Nature Publishing Group UK http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5722869/ http://www.ncbi.nlm.nih.gov/pubmed/29222424 http://dx.doi.org/10.1038/s41598-017-17677-4 © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. CC-BY Article Text 2017 ftpubmed https://doi.org/10.1038/s41598-017-17677-4 2017-12-17T01:14:18Z The family 15 carbohydrate esterase (CE15) MZ0003, which derives from a marine Arctic metagenome, has a broader substrate scope than other members of this family. Here we report the crystal structure of MZ0003, which reveals that residues comprising the catalytic triad differ from previously-characterized fungal homologs, and resolves three large loop regions that are unique to this bacterial sub-clade. The catalytic triad of the bacterial CE15, which includes Asp 332 as its third member, closely resembles that of family 1 carbohydrate esterases (CE1), despite the overall lower structural similarity with members of this family. Two of the three loop regions form a subdomain that deepens the active site pocket and includes several basic residues that contribute to the high positive charge surrounding the active site. Docking simulations predict specific interactions with the sugar moiety of glucuronic-acid substrates, and with aromatically-substituted derivatives that serve as model compounds for the lignin-carbohydrate complex of plant cell walls. Molecular dynamics simulations indicate considerable flexibility of the sub-domain in the substrate-bound form, suggesting plasticity to accommodate different substrates is possible. The findings from this first reported structure of a bacterial member of the CE15 family provide insight into the basis of its broader substrate specificity. Text Arctic PubMed Central (PMC) Arctic Scientific Reports 7 1 |
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Article De Santi, Concetta Gani, Osman ABSM Helland, Ronny Williamson, Adele Structural insight into a CE15 esterase from the marine bacterial metagenome |
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Article |
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The family 15 carbohydrate esterase (CE15) MZ0003, which derives from a marine Arctic metagenome, has a broader substrate scope than other members of this family. Here we report the crystal structure of MZ0003, which reveals that residues comprising the catalytic triad differ from previously-characterized fungal homologs, and resolves three large loop regions that are unique to this bacterial sub-clade. The catalytic triad of the bacterial CE15, which includes Asp 332 as its third member, closely resembles that of family 1 carbohydrate esterases (CE1), despite the overall lower structural similarity with members of this family. Two of the three loop regions form a subdomain that deepens the active site pocket and includes several basic residues that contribute to the high positive charge surrounding the active site. Docking simulations predict specific interactions with the sugar moiety of glucuronic-acid substrates, and with aromatically-substituted derivatives that serve as model compounds for the lignin-carbohydrate complex of plant cell walls. Molecular dynamics simulations indicate considerable flexibility of the sub-domain in the substrate-bound form, suggesting plasticity to accommodate different substrates is possible. The findings from this first reported structure of a bacterial member of the CE15 family provide insight into the basis of its broader substrate specificity. |
format |
Text |
author |
De Santi, Concetta Gani, Osman ABSM Helland, Ronny Williamson, Adele |
author_facet |
De Santi, Concetta Gani, Osman ABSM Helland, Ronny Williamson, Adele |
author_sort |
De Santi, Concetta |
title |
Structural insight into a CE15 esterase from the marine bacterial metagenome |
title_short |
Structural insight into a CE15 esterase from the marine bacterial metagenome |
title_full |
Structural insight into a CE15 esterase from the marine bacterial metagenome |
title_fullStr |
Structural insight into a CE15 esterase from the marine bacterial metagenome |
title_full_unstemmed |
Structural insight into a CE15 esterase from the marine bacterial metagenome |
title_sort |
structural insight into a ce15 esterase from the marine bacterial metagenome |
publisher |
Nature Publishing Group UK |
publishDate |
2017 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5722869/ http://www.ncbi.nlm.nih.gov/pubmed/29222424 https://doi.org/10.1038/s41598-017-17677-4 |
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Arctic |
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Arctic |
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Arctic |
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Arctic |
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5722869/ http://www.ncbi.nlm.nih.gov/pubmed/29222424 http://dx.doi.org/10.1038/s41598-017-17677-4 |
op_rights |
© The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
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CC-BY |
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https://doi.org/10.1038/s41598-017-17677-4 |
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Scientific Reports |
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