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The structure of a shellfish specific GST class glutathione S-transferase from antarctic bivalve Laternula elliptica reveals novel active site architecture

Cited 3 time in wos
Cited 3 time in scopus

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dc.contributor.authorPark, Ae-Kyung-
dc.contributor.authorChi, Young Min-
dc.contributor.authorLee, Ki Seog-
dc.contributor.authorAhn, In-Young-
dc.contributor.authorPark, Hyun-
dc.contributor.authorJang, Eun Hyuk-
dc.contributor.authorMoon, Jin Ho-
dc.date.accessioned2018-03-20T13:41:44Z-
dc.date.available2018-03-20T13:41:44Z-
dc.date.issued2013-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/6122-
dc.description.abstractGlutathione-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.iptica (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.-
dc.languageEnglish-
dc.publisherWilly-
dc.subjectBiochemistry & Molecular Biology-
dc.subjectBiophysics-
dc.titleThe structure of a shellfish specific GST class glutathione S-transferase from antarctic bivalve Laternula elliptica reveals novel active site architecture-
dc.title.alternative남극조개유래의 GST class glutathione S-transferase의 구조및 특성-
dc.typeArticle-
dc.identifier.bibliographicCitationPark, Ae-Kyung, et al. 2013. "The structure of a shellfish specific GST class glutathione S-transferase from antarctic bivalve Laternula elliptica reveals novel active site architecture". <em>PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS</em>, 81(3): 531-537.-
dc.citation.titlePROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS-
dc.citation.volume81-
dc.citation.number3-
dc.identifier.doi10.1002/prot.24208-
dc.citation.startPage531-
dc.citation.endPage537-
dc.description.articleClassificationSCI-
dc.description.jcrRateJCR 2011:37.24-
dc.subject.keywordLaternula elliptica-
dc.subject.keywordglutathione S-transferase-
dc.subject.keywordstructure-
dc.identifier.localId2013-0319-
dc.identifier.scopusid2-s2.0-84873087178-
dc.identifier.wosid000314179600017-
Appears in Collections  
2008-2010, Studies on Polar organisms and ecosystem changes (08-10) / Ahn, In-Young (PE09040, PE10040, PE08040)
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