Article
Structure, function and inhibition of the two- and three-domain 4Fe-4S IspG proteins.
Proceedings of the National Academy of Sciences of the United States of America - 29 May 2012
Liu Yi-Liang, Guerra Francisco, Wang Ke, Wang Weixue, Li Jikun, Huang Cancan, Zhu Wei, Houlihan Kevin, Li Zhi, Zhang Yong, Nair Satish K, Oldfield Eric
Abstract excerpt
IspG is a 4Fe4S protein involved in isoprenoid biosynthesis. Most bacterial IspGs contain two domains: a TIM barrel (A) and a 4Fe4S domain (B), but in plants and malaria parasites, there is a large insert domain (A*) whose structure and function are unknown. We show that bacterial IspGs function in solution as (AB)(2) dimers and that mutations in either both A or both B domains block activity. Chimeras harboring...
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