6a4w | pdb_00006a4w

AcrR from Mycobacterium tuberculosis

spinqualitylabelsall models 6a4w, resolution 2.59Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6a4w is a 2 chain structure with sequence from "bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, NA, SO4 Gene: acrR, ERS007657_03305, ERS007663_01106, ERS007670_02655, ERS007672_02023, ERS007679_02277, ERS007681_02293, ERS007688_01622, ERS007703_02625, ERS007722_01260, ERS023446_03575, ERS027646_00827, ERS027651_03158, ERS027653_04028, ERS027654_02941, ERS027659_02538, ERS027661_02360, ERS031537_01877, ERS124361_02153, SAMEA2682864_00974, SAMEA2683035_01767 ("Bacillus tuberculosis" (Zopf 1883) Klein 1884) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Transcriptional regulator proteins are closely involved in essential survival strategies in bacteria. AcrR is a one-component allosteric repressor of the genes associated with lipid transport and antibiotic resistance. When fatty acid ligands bind to the C-terminal ligand-binding cavity of AcrR, a conformational change in the N-terminal operator-binding region of AcrR is triggered, which releases the repressed DNA and initiates transcription. This paper focuses on the structural transition mechanism of AcrR of Mycobacterium tuberculosis upon DNA and ligand binding. AcrR loses its structural integrity upon ligand-mediated structural alteration and bends toward the promoter DNA in a more compact form, initiating a rotational motion. Our functional characterization of AcrR and description of the ligand- and DNA-recognition mechanism may facilitate the discovery of new therapies for tuberculosis. The crystal structure of AcrR from Mycobacterium tuberculosis reveals a one-component transcriptional regulation mechanism.,Kang SM, Kim DH, Jin C, Ahn HC, Lee BJ FEBS Open Bio. 2019 Oct;9(10):1713-1725. doi: 10.1002/2211-5463.12710. Epub 2019 , Aug 20. PMID:31369208 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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