4ooi | pdb_00004ooi

Reduced HlyU from Vibrio cholerae N16961

spinqualitylabelsall models 4ooi, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ooi is a 4 chain structure with sequence from Vibrio cholerae O1 biovar El Tor str. N16961. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HLYU_VIBCH Up-regulates the expression of the hemolysin gene, hlyA, and may promote expression of other virulence determinants in vivo. It may have both positive and negative regulator activities. Publication Abstract from PubMed HlyU in Vibrio cholerae is known to be the transcriptional activator of the hemolysin gene, HlyA and possibly a regulator of other virulence factors influencing growth, colonization and pathogenicity of this infective agent. Here we report the crystal structure of HlyU from V. cholerae N16961 (HlyU_Vc) at 1.8A. The protein, with five alpha-helices and three beta-strands in the topology of alpha1-alpha2-beta1-alpha3-alpha4-beta2-beta3-alpha5, forms a homodimer. Helices alpha3-alpha4 and a beta sheet form the winged helix-turn-helix (wHTH) DNA-binding motif common to the transcription regulators of the SmtB/ArsR family. In spite of an overall fold similar to SmtB/ArsR family, it lacks any metal binding site seen in SmtB. A comparison of the dimeric interfaces showed that the one in SmtB is much larger and have salt bridges that can be disrupted to accommodate metal ions. A model of HlyU-DNA complex suggests bending of the DNA. Cys38 in the structure was found to be modified as sulfenic acid; the oxidized form was not seen in another structure solved under reducing condition. Although devoid of any metal binding site, the presence of a Cys residue exhibiting oxidation-reduction suggests the possibility of the existence of a redox switch in transcription regulation. A structure-based phylogenetic analysis of wHTH proteins revealed the segregation of metal and non-metal binding proteins as well as those in the latter group that are under redox control. Crystal structure of HlyU, the hemolysin gene transcription activator, from Vibrio cholerae N16961 and functional implications.,Mukherjee D, Datta AB, Chakrabarti P Biochim Biophys Acta. 2014 Oct 18;1844(12):2346-2354. doi:, 10.1016/j.bbapap.2014.09.020. PMID:25450504 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transcriptional activator 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA