2XTZ
Crystal structure of the G alpha protein AtGPA1 from Arabidopsis thaliana
Summary for 2XTZ
| Entry DOI | 10.2210/pdb2xtz/pdb |
| Descriptor | GUANINE NUCLEOTIDE-BINDING PROTEIN ALPHA-1 SUBUNIT, MAGNESIUM ION, 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE, ... (6 entities in total) |
| Functional Keywords | hydrolase, g-protein signaling, self-activation, ras-like domain |
| Biological source | ARABIDOPSIS THALIANA (MOUSE-EAR CRESS) |
| Total number of polymer chains | 3 |
| Total formula weight | 125538.05 |
| Authors | Jones, J.C.,Duffy, J.W.,Machius, M.,Temple, B.R.S.,Dohlman, H.G.,Jones, A.M. (deposition date: 2010-10-13, release date: 2011-02-16, Last modification date: 2024-11-13) |
| Primary citation | Jones, J.C.,Duffy, J.W.,Machius, M.,Temple, B.R.S.,Dohlman, H.G.,Jones, A.M. The Crystal Structure of a Self-Activating G Protein Alpha Subunit Reveals its Distinct Mechanism of Signal Initiation Sci.Signal., 159:RA8-, 2011 Cited by PubMed Abstract: In animals, heterotrimeric guanine nucleotide-binding protein (G protein) signaling is initiated by G protein-coupled receptors (GPCRs), which activate G protein α subunits; however, the plant Arabidopsis thaliana lacks canonical GPCRs, and its G protein α subunit (AtGPA1) is self-activating. To investigate how AtGPA1 becomes activated, we determined its crystal structure. AtGPA1 is structurally similar to animal G protein α subunits, but our crystallographic and biophysical studies revealed that it had distinct properties. Notably, the helical domain of AtGPA1 displayed pronounced intrinsic disorder and a tendency to disengage from the Ras domain of the protein. Domain substitution experiments showed that the helical domain of AtGPA1 was necessary for self-activation and sufficient to confer self-activation to an animal G protein α subunit. These findings reveal the structural basis for a mechanism for G protein activation in Arabidopsis that is distinct from the well-established mechanism found in animals. PubMed: 21304159DOI: 10.1126/SCISIGNAL.2001446 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.34 Å) |
Structure validation
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