7kug | pdb_00007kug

Fe-S cluster-bound transcription activator WhiB7 in complex with the SigmaAr4-RNAP Beta flap tip chimera

spinqualitylabelsall models 7kug, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7kug is a 4 chain structure with sequence from Mycobacterium tuberculosis and Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.55Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed WhiB7 represents a distinct subclass of transcription factors in the WhiB-Like (Wbl) family, a unique group of iron-sulfur (4Fe-4S] cluster-containing proteins exclusive to the phylum of Actinobacteria. In Mycobacterium tuberculosis (Mtb), WhiB7 interacts with domain 4 of the primary sigma factor (sigma(A)(4)) in the RNA polymerase holoenzyme and activates genes involved in multiple drug resistance and redox homeostasis. Here, we report crystal structures of the WhiB7:sigma(A)(4) complex alone and bound to its target promoter DNA at 1.55-A and 2.6-A resolution, respectively. These structures show how WhiB7 regulates gene expression by interacting with both sigma(A)(4) and the AT-rich sequence upstream of the -35 promoter DNA via its C-terminal DNA-binding motif, the AT-hook. By combining comparative structural analysis of the two high-resolution sigma(A)(4)-bound Wbl structures with molecular and biochemical approaches, we identify the structural basis of the functional divergence between the two distinct subclasses of Wbl proteins in Mtb. Structural insights into the functional divergence of WhiB-like proteins in Mycobacterium tuberculosis.,Wan T, Horova M, Beltran DG, Li S, Wong HX, Zhang LM Mol Cell. 2021 Jul 15;81(14):2887-2900.e5. doi: 10.1016/j.molcel.2021.06.002. , Epub 2021 Jun 24. PMID:34171298 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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