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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

Authors
Park, Ae KyungMoon, Jin HoJang, Eun HyukPark, HyunAhn, In YoungLee, Ki SeogChi, Young Min
Issue Date
3월-2013
Publisher
WILEY
Keywords
Antarctic bivalve; Glutathione-S-transferases; Laternula elliptica; Marine organisms; Shellfish specific GST
Citation
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, v.81, no.3, pp.531 - 537
Indexed
SCIE
SCOPUS
Journal Title
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume
81
Number
3
Start Page
531
End Page
537
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/103785
DOI
10.1002/prot.24208
ISSN
0887-3585
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. (C) 2012 Wiley Periodicals, Inc.
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생명과학대학 (생명공학부)
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