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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 2 time in scopus
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Title
The structure of a shellfish specific GST class glutathione S-transferase from antarctic bivalve Laternula elliptica reveals novel active site architecture
Other Titles
남극조개유래의 GST class glutathione S-transferase의 구조및 특성
Authors
Park, Ae-Kyung
Chi, Young Min
Lee, Ki Seog
Ahn, In-Young
Park, Hyun
Jang, Eun Hyuk
Moon, Jin Ho
Subject
Biochemistry & Molecular Biology; Biophysics
Keywords
Laternula elliptica; glutathione S-transferase; structure
Issue Date
2013
Publisher
Willy
Citation
Park, 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". PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 81(3): 531-537.
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.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.
URI
http://repository.kopri.re.kr/handle/201206/6122
DOI
http://dx.doi.org/10.1002/prot.24208
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