The structure of a shellfish specific GST class glutathione S‐transferase from antarctic bivalve Laternula ellipticareveals novel active site architecture
Abstract Glutathione‐S‐transferases have been identified in all the living species examined so far, yet little is known about their function in marine organisms. In a previous report, the recently identified GST from Antarctic bivalve Laternula elliptica (LeGST) was classified into the rho class GST...
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Online Access: | http://dx.doi.org/10.1002/prot.24208 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fprot.24208 https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.24208 |
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crwiley:10.1002/prot.24208 2024-06-02T07:58:12+00:00 The structure of a shellfish specific GST class glutathione S‐transferase from antarctic bivalve Laternula ellipticareveals novel active site architecture Park, Ae Kyung Moon, Jin Ho Jang, Eun Hyuk Park, Hyun Ahn, In Young Lee, Ki Seog Chi, Young Min Korea Polar Research Institute 2012 http://dx.doi.org/10.1002/prot.24208 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fprot.24208 https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.24208 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Proteins: Structure, Function, and Bioinformatics volume 81, issue 3, page 531-537 ISSN 0887-3585 1097-0134 journal-article 2012 crwiley https://doi.org/10.1002/prot.24208 2024-05-06T06:58:03Z Abstract Glutathione‐S‐transferases have been identified in all the living species examined so far, yet little is known about their function in marine organisms. In a previous report, the recently identified GST from Antarctic bivalve Laternula elliptica (LeGST) was classified into the rho class GST, but there are several unique features of LeGST that may justify reclassification, which could represent specific shellfish GSTs. Here, we determined the crystal structure of LeGST, which is a shellfish specific class of GST. The structural analysis showed that the relatively open and wide hydrophobic H‐site of the LeGST allows this GST to accommodate various substrates. These results suggest that the H‐site of LeGST may be the result of adaptation to their environments as sedentary organisms. Proteins 2013. © 2012 Wiley Periodicals, Inc. Article in Journal/Newspaper Antarc* Antarctic Wiley Online Library Antarctic Rho ENVELOPE(-63.000,-63.000,-64.300,-64.300) Proteins: Structure, Function, and Bioinformatics 81 3 531 537 |
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Wiley Online Library |
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crwiley |
language |
English |
description |
Abstract Glutathione‐S‐transferases have been identified in all the living species examined so far, yet little is known about their function in marine organisms. In a previous report, the recently identified GST from Antarctic bivalve Laternula elliptica (LeGST) was classified into the rho class GST, but there are several unique features of LeGST that may justify reclassification, which could represent specific shellfish GSTs. Here, we determined the crystal structure of LeGST, which is a shellfish specific class of GST. The structural analysis showed that the relatively open and wide hydrophobic H‐site of the LeGST allows this GST to accommodate various substrates. These results suggest that the H‐site of LeGST may be the result of adaptation to their environments as sedentary organisms. Proteins 2013. © 2012 Wiley Periodicals, Inc. |
author2 |
Korea Polar Research Institute |
format |
Article in Journal/Newspaper |
author |
Park, Ae Kyung Moon, Jin Ho Jang, Eun Hyuk Park, Hyun Ahn, In Young Lee, Ki Seog Chi, Young Min |
spellingShingle |
Park, Ae Kyung Moon, Jin Ho Jang, Eun Hyuk Park, Hyun Ahn, In Young Lee, Ki Seog Chi, Young Min The structure of a shellfish specific GST class glutathione S‐transferase from antarctic bivalve Laternula ellipticareveals novel active site architecture |
author_facet |
Park, Ae Kyung Moon, Jin Ho Jang, Eun Hyuk Park, Hyun Ahn, In Young Lee, Ki Seog Chi, Young Min |
author_sort |
Park, Ae Kyung |
title |
The structure of a shellfish specific GST class glutathione S‐transferase from antarctic bivalve Laternula ellipticareveals novel active site architecture |
title_short |
The structure of a shellfish specific GST class glutathione S‐transferase from antarctic bivalve Laternula ellipticareveals novel active site architecture |
title_full |
The structure of a shellfish specific GST class glutathione S‐transferase from antarctic bivalve Laternula ellipticareveals novel active site architecture |
title_fullStr |
The structure of a shellfish specific GST class glutathione S‐transferase from antarctic bivalve Laternula ellipticareveals novel active site architecture |
title_full_unstemmed |
The structure of a shellfish specific GST class glutathione S‐transferase from antarctic bivalve Laternula ellipticareveals novel active site architecture |
title_sort |
structure of a shellfish specific gst class glutathione s‐transferase from antarctic bivalve laternula ellipticareveals novel active site architecture |
publisher |
Wiley |
publishDate |
2012 |
url |
http://dx.doi.org/10.1002/prot.24208 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fprot.24208 https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.24208 |
long_lat |
ENVELOPE(-63.000,-63.000,-64.300,-64.300) |
geographic |
Antarctic Rho |
geographic_facet |
Antarctic Rho |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Proteins: Structure, Function, and Bioinformatics volume 81, issue 3, page 531-537 ISSN 0887-3585 1097-0134 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/prot.24208 |
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Proteins: Structure, Function, and Bioinformatics |
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81 |
container_issue |
3 |
container_start_page |
531 |
op_container_end_page |
537 |
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1800741478523207680 |