2w1r

Crystal Structure of the C-terminal Domain of B. subtilis SpoVT

spinqualitylabelsall models 2w1r, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2w1r is a 1 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.5Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SPOVT_BACSU Transcriptional factor that regulates positively or negatively the expression of a large number of forespore-specific sigma G-dependent genes. May provide a mechanism of feedback control that is important for forespore development (PubMed:8755877). SpoVT levels during spore formation have a major impact on the germination and the resistance of the resultant spores (PubMed:22522895). Publication Abstract from PubMed 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. Crystal Structure of SpoVT, the Final Modulator of Gene Expression during Spore Development in Bacillus subtilis.,Asen I, Djuranovic S, Lupas AN, Zeth K J Mol Biol. 2008 Oct 30. PMID:18996130 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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