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Acta Crystallogr F Struct Biol Commun. 2014 Jan;70(Pt 1):113-5. doi: 10.1107/S2053230X13033645. Epub 2013 Dec 24.

Purification, crystallization and preliminary X-ray crystallographic analysis of a rice Rac/Rop GTPase, OsRac1.

Author information

1
Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
2
Laboratory of Biophysics, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan.
3
Laboratory of Plant Molecular Genetics, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan.

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.

KEYWORDS:

GTP-binding form; OsRac1; small GTPase

PMID:
24419631
PMCID:
PMC3943088
DOI:
10.1107/S2053230X13033645
[Indexed for MEDLINE]
Free PMC Article

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