2W1R
Crystal Structure of the C-terminal Domain of B. subtilis SpoVT
Summary for 2W1R
| Entry DOI | 10.2210/pdb2w1r/pdb |
| Related | 2W1T |
| Descriptor | STAGE V SPORULATION PROTEIN T (2 entities in total) |
| Functional Keywords | regulatory gaf domain of spovt, transcription, transcription regulation, repressor, activator, sporulation, dna-binding |
| Biological source | BACILLUS SUBTILIS |
| Total number of polymer chains | 1 |
| Total formula weight | 13396.90 |
| Authors | Asen, I.,Djuranovic, S.,Lupas, A.N.,Zeth, K. (deposition date: 2008-10-20, release date: 2008-11-18, Last modification date: 2024-05-08) |
| Primary citation | Asen, I.,Djuranovic, S.,Lupas, A.N.,Zeth, K. Crystal Structure of Spovt, the Final Modulator of Gene Expression During Spore Development in Bacillus Subtilis J.Mol.Biol., 386:962-, 2009 Cited by PubMed Abstract: Endospore formation in Bacillus subtilis is orchestrated by five developmental sigma factors and further modulated by several auxiliary transcription factors. One of these, SpoVT, regulates forespore-specific sigma(G)-dependent genes and plays a key role in the final stages of spore formation. We have determined the crystal structure of the isolated C-terminal domain of SpoVT at 1.5 A by experimental phasing techniques and used this model to solve the structure of the full-length SpoVT at 2.6 A by molecular replacement. SpoVT is a tetramer that shows an overall significant distortion mediated by electrostatic interactions. Two monomers dimerize via the highly charged N-terminal domains to form swapped-hairpin beta-barrels. These asymmetric dimers further tetramerize through the formation of mixed helix bundles between their C-terminal domains, which themselves fold as GAF (cGMP-specific and cGMP-stimulated phosphodiesterases, Anabaena adenylate cyclases, and Escherichia coli FhlA) domains. The combination of a swapped-hairpin beta-barrel with a GAF domain represents a novel domain architecture in transcription factors. The occurrence of SpoVT homologs throughout Bacilli and Clostridia demonstrates the ancestral origin of this factor in sporulation. PubMed: 18996130DOI: 10.1016/J.JMB.2008.10.061 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
Download full validation report
