2Z0Q
Crystal structure of DH-PH domain of RhoGEF3(Xpln)
Summary for 2Z0Q
| Entry DOI | 10.2210/pdb2z0q/pdb |
| Descriptor | Rho guanine nucleotide exchange factor 3, SULFATE ION (3 entities in total) |
| Functional Keywords | dh-ph domain, guanine-nucleotide releasing factor, signaling protein, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Cytoplasm: Q91X46 |
| Total number of polymer chains | 1 |
| Total formula weight | 40734.60 |
| Authors | Murayama, K.,Kato-Murayama, M.,Terada, T.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2007-05-07, release date: 2008-05-13, Last modification date: 2012-12-12) |
| Primary citation | Murayama, K.,Kato-Murayama, M.,Akasaka, R.,Terada, T.,Yokoyama, S.,Shirouzu, M. Structure of the Rho-specific guanine nucleotide-exchange factor Xpln Acta Crystallogr.,Sect.F, 68:1455-1459, 2012 Cited by PubMed Abstract: Xpln is a guanine nucleotide-exchange factor (GEF) for Rho GTPases. A Dbl homology (DH) domain followed by a pleckstrin homology (PH) domain is a widely adopted GEF-domain architecture. The Xpln structure solely comprises these two domains. Xpln activates RhoA and RhoB, but not RhoC, although their GTPase sequences are highly conserved. The molecular mechanism of the selectivity of Xpln for Rho GTPases is still unclear. In this study, the crystal structure of the tandemly arranged DH-PH domains of mouse Xpln, with a single molecule in the asymmetric unit, was determined at 1.79 Å resolution by the multiwavelength anomalous dispersion method. The DH-PH domains of Xpln share high structural similarity with those from neuroepithelial cell-transforming gene 1 protein, PDZ-RhoGEF, leukaemia-associated RhoGEF and intersectins 1 and 2. The crystal structure indicated that the α4-α5 loop in the DH domain is flexible and that the DH and PH domains interact with each other intramolecularly, thus suggesting that PH-domain rearrangement occurs upon RhoA binding. PubMed: 23192023DOI: 10.1107/S1744309112045265 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.79 Å) |
Structure validation
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