4nn1 | pdb_00004nn1

Crystal Structure of transcriptional regulator Rv1219c of Mycobacterium tuberculosis

spinqualitylabelsall models 4nn1, resolution 2.99Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4nn1 is a 1 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RAAS_MYCTU Regulates the expression of the Rv1217c-Rv1218c multidrug efflux system and its own expression. Acts by binding to promoter regions of Rv1219c and upstream of the Rv1218c gene (PubMed:24424575). Important for survival in prolonged stationary phase and during macrophage infection (PubMed:24590482). May be used to eliminate non-growing mycobacteria (PubMed:25012658). Publication Abstract from PubMed The Rv1217c-Rv1218c multidrug efflux system, which belongs to the ATP-binding cassette (ABC) superfamily, recognizes and actively extrudes a variety of structurally unrelated toxic chemicals and mediates the intrinsic resistance to these antimicrobials in Mycobacterium tuberculosis. The expression of Rv1217c-Rv1218c is controlled by the TetR-like transcriptional regulator Rv1219c, which is encoded by a gene immediately upstream of rv1218c. To elucidate the structural basis of Rv1219c regulation, we have determined the crystal structure of Rv1219c, which reveals a dimeric two-domain molecule with an entirely helical architecture similar to members of the TetR family of transcriptional regulators. The N-terminal domains of the Rv1219c dimer are separated by a large center-to-center distance of 64 A. The C-terminal domain of each protomer possesses a large cavity. Docking of small compounds to Rv1219c suggests that this large cavity forms a multidrug binding pocket, which can accommodate a variety of structurally unrelated antimicrobial agents. The internal wall of the multidrug binding site is surrounded by seven aromatic residues, indicating that drug binding may be governed by aromatic stacking interactions. In addition, fluorescence polarization reveals that Rv1219c binds drugs in the micromolar range. Crystal Structure of the transcriptional regulator Rv1219c of Mycobacterium tuberculosis.,Kumar N, Radhakrishnan A, Wright CC, Chou TH, Lei HT, Bolla JR, Tringides ML, Rajashankar KR, Su CC, Purdy GE, Yu EW Protein Sci. 2014 Jan 14. doi: 10.1002/pro.2424. PMID:24424575 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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