Open AccessStructure of the GDP‐bound G domain of the RGK protein Rem2
Author(s) -
Reymond Philippe,
Coquard Aline,
Che Mélanie,
Zeghouf Mahel,
El Marjou Ahmed,
Thompson Andrew,
Ménétrey Julie
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112013541
Subject(s) - gtp' , protein structure , chemistry , gtpase , guanosine diphosphate , biology , biophysics , crystallography , microbiology and biotechnology , biochemistry , guanosine triphosphate , enzyme
RGK proteins are atypical small GTP‐binding proteins that are involved in the regulation of voltage‐dependent calcium channels and actin cytoskeleton remodelling. The structure of the Rem2 G domain bound to GDP is reported here in a monoclinic crystal form at 2.66 Å resolution. It is very similar to the structure determined previously from an orthorhombic crystal form. However, differences in the crystal‐packing environment revealed that the switch I and switch II regions are flexible and not ordered as previously reported. Comparison of the available RGK protein structures along with those of other small GTP‐binding proteins highlights two structural features characteristic of this atypical family and suggests that the conserved tryptophan residue in the D X WE X motif may be a structural determinant of the nucleotide‐binding affinity.