PDBsum entry 5cm9

Signaling protein

PDB id: 5cm9

Contents

Protein chains

405 a.a.

146 a.a.

Waters ×36

PDB id:

5cm9

Name:

Signaling protein

Title:

Structural basis for the selectivity of guanine nucleotide exchange factors for the small g-protein ral

Structure:

Ral guanine nucleotide dissociation stimulator-like 2. Chain: a, b. Synonym: ralgds-like 2,ralgds-like factor,ras-associated protein rab2l. Engineered: yes. Ras-related protein ral-a. Chain: c, d. Engineered: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: rgl2, rab2l, rlf. Expressed in: escherichia coli. Expression_system_taxid: 562. Drosophila melanogaster. Fruit fly. Organism_taxid: 7227.

Resolution:

2.60Å R-factor: 0.276 R-free: 0.320

Authors:

M.Popovic,A.Schouten,H.Rehmann

Key ref:

M.Popovic et al. (2016). 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. PubMed id: 26687416 DOI: 10.1016/j.jsb.2015.12.006

Date:

16-Jul-15 Release date: 13-Jan-16

Protein chains

Q61193  (RGL2_MOUSE) -  Ral guanine nucleotide dissociation stimulator-like 2 from Mus musculus

Seq: 778 a.a.

Struc: 405 a.a.*

Protein chains

P48555  (RALA_DROME) -  Ras-related protein Ral-a from Drosophila melanogaster

Seq: 201 a.a.

Struc: 146 a.a.

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class 2: Chains A, B: E.C.?
• Enzyme class 3: Chains C, D: E.C.3.6.5.2 - small monomeric GTPase.
• Reaction: GTP + H2O = GDP + phosphate + H⁺

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.jsb.2015.12.006

J Struct Biol 193:106-114 (2016)

PubMed id: 26687416

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.

M.Popovic, A.Schouten, M.Rensen-de Leeuw, H.Rehmann.

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.