3QAV

Crystal structure of a glutathione S-transferase from Antarctic clam Laternula elliptica

Summary for 3QAV

• Entry DOI: 10.2210/pdb3qav/pdb
• Related: 3QAW
• Descriptor: Rho-class glutathione S-transferase (2 entities in total)
• Functional Keywords: cytosol, transferase
• Biological source: Laternula elliptica
• Total number of polymer chains: 1
• Total formula weight: 27981.18

Authors

Park, A.K.,Moon, J.H.,Chi, Y.M. (deposition date: 2011-01-12, release date: 2012-02-01, Last modification date: 2024-03-20)

Primary citation

Park, A.K.,Moon, J.H.,Jang, E.H.,Park, H.,Ahn, I.Y.,Lee, K.S.,Chi, Y.M.
The structure of a shellfish specific GST class glutathione S-transferase from antarctic bivalve Laternula elliptica reveals novel active site architecture.
Proteins, 81:531-537, 2013

PubMed 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.

PubMed: 23152139
DOI: 10.1002/prot.24208

Experimental method

X-RAY DIFFRACTION (2.1 Å)