| Literature DB >> 24419631 |
Ken-ichi Kosami1, Izuru Ohki2, Kokoro Hayashi2, Ryo Tabata2, Sayaka Usugi2, Tsutomu Kawasaki3, Toshimichi Fujiwara1, Atsushi Nakagawa1, Ko Shimamoto3, Chojiro Kojima1.
Abstract
Small GTPases regulate a large variety of key cellular processes. Plant small Rac/Rop GTPases have recently received broad attention as it is becoming clear that these enzymes regulate various plant cellular processes. OsRac1, a rice Rac/Rop protein, is a key regulator of reactive oxygen species (ROS) production and induces immune responses. Although four structures of plant small GTPases have been reported, all of these were of the inactive form. Here, OsRac1 was purified and co-crystallized with the GTP analogue 5'-guanylyl imidodiphosphate (GMPPNP). The crystal belonged to space group P2(1)2(1)2(1) and a complete data set was collected to 1.9 Å resolution.Entities:
Keywords: GTP-binding form; OsRac1; small GTPase
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Year: 2013 PMID: 24419631 PMCID: PMC3943088 DOI: 10.1107/S2053230X13033645
Source DB: PubMed Journal: Acta Crystallogr F Struct Biol Commun ISSN: 2053-230X Impact factor: 1.056