Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2015 Dec 4;291(10):5234–5246. doi: 10.1074/jbc.M115.694307

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2016 by The American Society for Biochemistry and Molecular Biology, Inc.

Author's Choice—Final version free via Creative Commons CC-BY license.

PMC Copyright notice

FIGURE 4. — Representative cytosolic GST dimer forms. Representatives from several GST classes are shown, in which one molecule of the dimer is shown in brown, the second molecule of the dimer is shown in rainbow colors (N terminus in blue to C terminus in red), and the bound glutathione or glutathione analog is shown as yellow spheres. The Alpha (Protein Data Bank entry 1GUH; human GST A1-1), Mu (2GST; rat), Pi (2GSR; pGST P1-1 from pig), Sigma (1GSQ; squid), Theta (1LJR; human hGST T2-2), Beta (2PMT; bacterial GST from P. mirabilis), Omega (3LFL; human GST Omega-1), and LigG (4G10; Sphingobium sp. SYK-6) dimers show variations on the α3/α4 canonical four-helix bundle dimer structure, whereas the GSTFuA structure from P. chrysosporium shows a non-canonical dimer formed via interaction between α4 and the C-terminal domain of the second molecule of the dimer.