Structural and biochemical insights into PsEst3, a new GHSR-type esterase obtained from Paenibacillus sp. R4
PsEst3, a psychrophilic esterase obtained from Paenibacillus sp. R4, which was isolated from the permafrost of Alaska, exhibits relatively high activity at low temperatures. Here, crystal structures of PsEst3 complexed with various ligands were generated and studied at atomic resolution, and biochem...
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ftpubmed:oai:pubmedcentral.nih.gov:9980389 2023-05-15T17:57:55+02:00 Structural and biochemical insights into PsEst3, a new GHSR-type esterase obtained from Paenibacillus sp. R4 Son, Jonghyeon Choi, Woong Kim, Hyun Kim, Minseo Lee, Jun Hyuck Shin, Seung Chul Kim, Han-Woo 2023-02-28 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9980389/ http://www.ncbi.nlm.nih.gov/pubmed/36862488 https://doi.org/10.1107/S2052252523001562 en eng International Union of Crystallography http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9980389/ http://www.ncbi.nlm.nih.gov/pubmed/36862488 http://dx.doi.org/10.1107/S2052252523001562 © Jonghyeon Son et al. 2023 https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. CC-BY IUCrJ Research Papers Text 2023 ftpubmed https://doi.org/10.1107/S2052252523001562 2023-03-05T02:52:49Z PsEst3, a psychrophilic esterase obtained from Paenibacillus sp. R4, which was isolated from the permafrost of Alaska, exhibits relatively high activity at low temperatures. Here, crystal structures of PsEst3 complexed with various ligands were generated and studied at atomic resolution, and biochemical studies were performed to analyze the structure–function relationship of PsEst3. Certain unique characteristics of PsEst3 distinct from those of other classes of lipases/esterases were identified. Firstly, PsEst3 contains a conserved GHSRA/G pentapeptide sequence in the GxSxG motif around the nucleophilic serine. Additionally, it contains a conserved HGFR/K consensus sequence in the oxyanion hole, which is distinct from that in other lipase/esterase families, as well as a specific domain composition (for example a helix–turn–helix motif) and a degenerative lid domain that exposes the active site to the solvent. Secondly, the electrostatic potential of the active site in PsEst3 is positive, which may cause unintended binding of negatively charged chemicals in the active site. Thirdly, the last residue of the oxyanion hole-forming sequence, Arg44, separates the active site from the solvent by sealing the acyl-binding pocket, suggesting that PsEst3 is an enzyme that is customized to sense an unidentified substrate that is distinct from those of classical lipases/esterases. Collectively, this evidence strongly suggests that PsEst3 belongs to a distinct family of esterases. Text permafrost Alaska PubMed Central (PMC) IUCrJ 10 2 220 232 |
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Research Papers Son, Jonghyeon Choi, Woong Kim, Hyun Kim, Minseo Lee, Jun Hyuck Shin, Seung Chul Kim, Han-Woo Structural and biochemical insights into PsEst3, a new GHSR-type esterase obtained from Paenibacillus sp. R4 |
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Research Papers |
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PsEst3, a psychrophilic esterase obtained from Paenibacillus sp. R4, which was isolated from the permafrost of Alaska, exhibits relatively high activity at low temperatures. Here, crystal structures of PsEst3 complexed with various ligands were generated and studied at atomic resolution, and biochemical studies were performed to analyze the structure–function relationship of PsEst3. Certain unique characteristics of PsEst3 distinct from those of other classes of lipases/esterases were identified. Firstly, PsEst3 contains a conserved GHSRA/G pentapeptide sequence in the GxSxG motif around the nucleophilic serine. Additionally, it contains a conserved HGFR/K consensus sequence in the oxyanion hole, which is distinct from that in other lipase/esterase families, as well as a specific domain composition (for example a helix–turn–helix motif) and a degenerative lid domain that exposes the active site to the solvent. Secondly, the electrostatic potential of the active site in PsEst3 is positive, which may cause unintended binding of negatively charged chemicals in the active site. Thirdly, the last residue of the oxyanion hole-forming sequence, Arg44, separates the active site from the solvent by sealing the acyl-binding pocket, suggesting that PsEst3 is an enzyme that is customized to sense an unidentified substrate that is distinct from those of classical lipases/esterases. Collectively, this evidence strongly suggests that PsEst3 belongs to a distinct family of esterases. |
format |
Text |
author |
Son, Jonghyeon Choi, Woong Kim, Hyun Kim, Minseo Lee, Jun Hyuck Shin, Seung Chul Kim, Han-Woo |
author_facet |
Son, Jonghyeon Choi, Woong Kim, Hyun Kim, Minseo Lee, Jun Hyuck Shin, Seung Chul Kim, Han-Woo |
author_sort |
Son, Jonghyeon |
title |
Structural and biochemical insights into PsEst3, a new GHSR-type esterase obtained from Paenibacillus sp. R4 |
title_short |
Structural and biochemical insights into PsEst3, a new GHSR-type esterase obtained from Paenibacillus sp. R4 |
title_full |
Structural and biochemical insights into PsEst3, a new GHSR-type esterase obtained from Paenibacillus sp. R4 |
title_fullStr |
Structural and biochemical insights into PsEst3, a new GHSR-type esterase obtained from Paenibacillus sp. R4 |
title_full_unstemmed |
Structural and biochemical insights into PsEst3, a new GHSR-type esterase obtained from Paenibacillus sp. R4 |
title_sort |
structural and biochemical insights into psest3, a new ghsr-type esterase obtained from paenibacillus sp. r4 |
publisher |
International Union of Crystallography |
publishDate |
2023 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9980389/ http://www.ncbi.nlm.nih.gov/pubmed/36862488 https://doi.org/10.1107/S2052252523001562 |
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permafrost Alaska |
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permafrost Alaska |
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IUCrJ |
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9980389/ http://www.ncbi.nlm.nih.gov/pubmed/36862488 http://dx.doi.org/10.1107/S2052252523001562 |
op_rights |
© Jonghyeon Son et al. 2023 https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. |
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CC-BY |
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https://doi.org/10.1107/S2052252523001562 |
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