Ontology highlight
ABSTRACT:
SUBMITTER: Guo Z
PROVIDER: S-EPMC2543052 | biostudies-literature | 2008 Sep
REPOSITORIES: biostudies-literature
Guo Zhong Z Guo Zhong Z Wu Yao-Wen YW Das Debapratim D Delon Christine C Cramer Janinna J Yu Shen S Thuns Sandra S Lupilova Nataliya N Waldmann Herbert H Brunsveld Luc L Goody Roger S RS Alexandrov Kirill K Blankenfeldt Wulf W
The EMBO journal 20080828 18
Post-translational isoprenylation of proteins is carried out by three related enzymes: farnesyltransferase, geranylgeranyl transferase-I, and Rab geranylgeranyl transferase (RabGGTase). Despite the fact that the last one is responsible for the largest number of individual protein prenylation events in the cell, no structural information is available on its interaction with substrates and products. Here, we present structural and biophysical analyses of RabGGTase in complex with phosphoisoprenoid ...[more]