4AII

Crystal structure of the rat REM2 GTPase - G domain bound to GDP

Summary for 4AII

• Entry DOI: 10.2210/pdb4aii/pdb
• Descriptor: GTP-BINDING PROTEIN REM 2, MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: gtp-binding protein, rgk proteins
• Biological source: RATTUS NORVEGICUS (NORWAY RAT)
• Cellular location: Cell membrane: Q9WTY2
• Total number of polymer chains: 2
• Total formula weight: 41242.39

Authors

Reymond, P.,Coquard, A.,Chenon, M.,Zeghouf, M.,El Marjou, A.,Thompson, A.,Menetrey, J. (deposition date: 2012-02-10, release date: 2012-06-13, Last modification date: 2023-12-20)

Primary citation

Reymond, P.,Coquard, A.,Chenon, M.,Zeghouf, M.,El Marjou, A.,Thompson, A.,Menetrey, J.
Structure of the Gdp-Bound G Domain of the Rgk Protein Rem2.
Acta Crystallogr.,Sect.F, 68:626-, 2012

PubMed Abstract: 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 DXWEX motif may be a structural determinant of the nucleotide-binding affinity.

PubMed: 22684057
DOI: 10.1107/S1744309112013541

Experimental method

X-RAY DIFFRACTION (2.66 Å)