5CM8

Structural Basis for the Selectivity of Guanine Nucleotide Exchange Factors for the small G-protein Ral

Summary for 5CM8

• Entry DOI: 10.2210/pdb5cm8/pdb
• Related: 5CM9
• Descriptor: Ral guanine nucleotide dissociation stimulator-like 2, Ras-related protein Ral-a (3 entities in total)
• Functional Keywords: complex g-protein exchange factor, signaling protein
• Biological source: Mus musculus (House Mouse); More
• Cellular location: Cell membrane ; Lipid-anchor ; Cytoplasmic side : P48555
• Total number of polymer chains: 2
• Total formula weight: 75231.18

Authors

Popovic, M.,Schouten, A.,Rehmann, H. (deposition date: 2015-07-16, release date: 2016-01-13, Last modification date: 2024-01-10)

Primary citation

Popovic, M.,Schouten, A.,Rensen-de Leeuw, M.,Rehmann, H.
The structure of the Guanine Nucleotide Exchange Factor Rlf in complex with the small G-protein Ral identifies conformational intermediates of the exchange reaction and the basis for the selectivity.
J.Struct.Biol., 193:106-114, 2016

PubMed Abstract: CDC25 homology domain (CDC25-HD) containing Guanine Nucleotide Exchange Factors (GEFs) initiate signalling by small G-proteins of the Ras-family. Each GEF acts on a small subset of the G-proteins only, thus providing signalling selectivity. Rlf is a GEF with selectivity for the G-proteins RalA and RalB. Here the crystal structure of Rlf in complex with Ral is determined. The Rlf·Ral complex crystallised into two different crystal forms, which represent different steps of the exchange reaction. Thereby general insight in the CDC25-HD catalysed nucleotide exchange is obtained. In addition, the basis for the selectivity of the interaction is investigated. The exchange activity is monitored by the use of recombinant proteins. Selectivity determinants in the binding interface are identified and confirmed by a mutational study.

PubMed: 26687416
DOI: 10.1016/j.jsb.2015.12.006

Experimental method

X-RAY DIFFRACTION (2.6 Å)