Structural determinants of cold activity and glucose tolerance of a family 1 glycoside hydrolase ( GH1) from Antarctic Marinomonas sp. ef1
Cold‐active enzymes support life at low temperatures due to their ability to maintain high activity in the cold and can be useful in several biotechnological applications. Although information on the mechanisms of enzyme cold adaptation is still too limited to devise general rules, it appears that v...
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Online Access: | http://dx.doi.org/10.1111/febs.17096 https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/febs.17096 |
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crwiley:10.1111/febs.17096 2024-09-09T19:06:28+00:00 Structural determinants of cold activity and glucose tolerance of a family 1 glycoside hydrolase ( GH1) from Antarctic Marinomonas sp. ef1 Gourlay, Louise Jane Mangiagalli, Marco Moroni, Elisabetta Lotti, Marina Nardini, Marco Università degli Studi di Milano 2024 http://dx.doi.org/10.1111/febs.17096 https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/febs.17096 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor The FEBS Journal volume 291, issue 13, page 2897-2917 ISSN 1742-464X 1742-4658 journal-article 2024 crwiley https://doi.org/10.1111/febs.17096 2024-08-06T04:15:04Z Cold‐active enzymes support life at low temperatures due to their ability to maintain high activity in the cold and can be useful in several biotechnological applications. Although information on the mechanisms of enzyme cold adaptation is still too limited to devise general rules, it appears that very diverse structural and functional changes are exploited in different protein families and within the same family. In this context, we studied the cold adaptation mechanism and the functional properties of a member of the glycoside hydrolase family 1 (GH1) from the Antarctic bacterium Marinomonas sp. ef1. This enzyme exhibits all typical functional hallmarks of cold adaptation, including high catalytic activity at 5 °C, broad substrate specificity, low thermal stability, and higher lability of the active site compared to the overall structure. Analysis of the here‐reported crystal structure (1.8 Å resolution) and molecular dynamics simulations suggest that cold activity and thermolability may be due to a flexible region around the active site (residues 298–331), whereas the dynamic behavior of loops flanking the active site (residues 47–61 and 407–413) may favor enzyme‐substrate interactions at the optimal temperature of catalysis ( T opt ) by tethering together protein regions lining the active site. Stapling of the N‐terminus onto the surface of the β‐barrel is suggested to partly counterbalance protein flexibility, thus providing a stabilizing effect. The tolerance of the enzyme to glucose and galactose is accounted for by the presence of a “gatekeeping” hydrophobic residue (Leu178), located at the entrance of the active site. Article in Journal/Newspaper Antarc* Antarctic Wiley Online Library Antarctic The Antarctic The FEBS Journal |
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Wiley Online Library |
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crwiley |
language |
English |
description |
Cold‐active enzymes support life at low temperatures due to their ability to maintain high activity in the cold and can be useful in several biotechnological applications. Although information on the mechanisms of enzyme cold adaptation is still too limited to devise general rules, it appears that very diverse structural and functional changes are exploited in different protein families and within the same family. In this context, we studied the cold adaptation mechanism and the functional properties of a member of the glycoside hydrolase family 1 (GH1) from the Antarctic bacterium Marinomonas sp. ef1. This enzyme exhibits all typical functional hallmarks of cold adaptation, including high catalytic activity at 5 °C, broad substrate specificity, low thermal stability, and higher lability of the active site compared to the overall structure. Analysis of the here‐reported crystal structure (1.8 Å resolution) and molecular dynamics simulations suggest that cold activity and thermolability may be due to a flexible region around the active site (residues 298–331), whereas the dynamic behavior of loops flanking the active site (residues 47–61 and 407–413) may favor enzyme‐substrate interactions at the optimal temperature of catalysis ( T opt ) by tethering together protein regions lining the active site. Stapling of the N‐terminus onto the surface of the β‐barrel is suggested to partly counterbalance protein flexibility, thus providing a stabilizing effect. The tolerance of the enzyme to glucose and galactose is accounted for by the presence of a “gatekeeping” hydrophobic residue (Leu178), located at the entrance of the active site. |
author2 |
Università degli Studi di Milano |
format |
Article in Journal/Newspaper |
author |
Gourlay, Louise Jane Mangiagalli, Marco Moroni, Elisabetta Lotti, Marina Nardini, Marco |
spellingShingle |
Gourlay, Louise Jane Mangiagalli, Marco Moroni, Elisabetta Lotti, Marina Nardini, Marco Structural determinants of cold activity and glucose tolerance of a family 1 glycoside hydrolase ( GH1) from Antarctic Marinomonas sp. ef1 |
author_facet |
Gourlay, Louise Jane Mangiagalli, Marco Moroni, Elisabetta Lotti, Marina Nardini, Marco |
author_sort |
Gourlay, Louise Jane |
title |
Structural determinants of cold activity and glucose tolerance of a family 1 glycoside hydrolase ( GH1) from Antarctic Marinomonas sp. ef1 |
title_short |
Structural determinants of cold activity and glucose tolerance of a family 1 glycoside hydrolase ( GH1) from Antarctic Marinomonas sp. ef1 |
title_full |
Structural determinants of cold activity and glucose tolerance of a family 1 glycoside hydrolase ( GH1) from Antarctic Marinomonas sp. ef1 |
title_fullStr |
Structural determinants of cold activity and glucose tolerance of a family 1 glycoside hydrolase ( GH1) from Antarctic Marinomonas sp. ef1 |
title_full_unstemmed |
Structural determinants of cold activity and glucose tolerance of a family 1 glycoside hydrolase ( GH1) from Antarctic Marinomonas sp. ef1 |
title_sort |
structural determinants of cold activity and glucose tolerance of a family 1 glycoside hydrolase ( gh1) from antarctic marinomonas sp. ef1 |
publisher |
Wiley |
publishDate |
2024 |
url |
http://dx.doi.org/10.1111/febs.17096 https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/febs.17096 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
The FEBS Journal volume 291, issue 13, page 2897-2917 ISSN 1742-464X 1742-4658 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1111/febs.17096 |
container_title |
The FEBS Journal |
_version_ |
1809820524266651648 |