Nicholas C. Price
University of Strathclyde
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Journal of Biological Chemistry | 1997
M. W. Kennedy; Lisa H. Garside; Lucy E. Goodrick; Lindsay McDermott; Andy Brass; Nicholas C. Price; Sharon M. Kelly; Alan Cooper; Jannette E. Bradley
Ov20 is a major antigen of the parasitic nematodeOnchocerca volvulus, the causative agent of river blindness in humans, and the protein is secreted into the tissue occupied by the parasite. DNA encoding Ov20 was isolated, and the protein was expressed in Escherichia coli. Fluorescence-based ligand binding assays show that the protein contains a high affinity binding site for retinol, fluorescent fatty acids (11-((5-dimethylaminonaphthalene-1-sulfonyl)amino)undecanoic acid, dansyl-dl-α-aminocaprylic acid, and parinaric acid) and, by competition, oleic and arachidonic acids, but not cholesterol. The fluorescence emission of dansylated fatty acids is significantly blue-shifted upon binding in comparison to similarly sized β-sheet-rich mammalian retinol- and fatty acid-binding proteins. Secondary structure prediction algorithms indicate that a α-helix predominates in Ov20, possibly in a coiled coil motif, with no evidence of β structures, and this was confirmed by circular dichroism. The protein is highly stable in solution, requiring temperatures in excess of 90 °C or high denaturant concentrations for unfolding. Ov20 therefore represents a novel class of small retinol-binding protein, which appears to be confined to nematodes. The retinol binding activity of Ov20 could possibly contribute to the eye defects associated with onchocerciasis and, because there is no counterpart in mammals, represents a strategic target for chemotherapy.
Journal of Inorganic Biochemistry | 2002
Kirsty J. McLean; Myles R. Cheesman; Stuart L Rivers; Alison Richmond; David Leys; Stephen K. Chapman; Graeme A Reid; Nicholas C. Price; Sharon M. Kelly; John Clarkson; W. Ewen Smith; Andrew W. Munro
The CYP121 gene from the pathogenic bacterium Mycobacterium tuberculosis has been cloned and expressed in Escherichia coli, and the protein purified to homogeneity by ion exchange and hydrophobic interaction chromatography. The CYP121 gene encodes a cytochrome P450 enzyme (CYP121) that displays typical electronic absorption features for a member of this superfamily of hemoproteins (major Soret absorption band at 416.5 nm with alpha and beta bands at 565 and 538 nm, respectively, in the oxidized form) and which binds carbon monoxide to give the characteristic Soret band shift to 448 nm. Resonance Raman, EPR and MCD spectra show the protein to be predominantly low-spin and to have a typical cysteinate- and water-ligated b-type heme iron. CD spectra in the far UV region describe a mainly alpha helical conformation, but the visible CD spectrum shows a band of positive sign in the Soret region, distinct from spectra for other P450s recognized thus far. CYP121 binds very tightly to a range of azole antifungal drugs (e.g. clotrimazole, miconazole), suggesting that it may represent a novel target for these antibiotics in the M. tuberculosis pathogen.
Journal of Biological Chemistry | 2003
Louise J. Gourlay; David Bhella; Sharon M. Kelly; Nicholas C. Price; J. Gordon Lindsay
Bovine mitochondrial SP-22 is a member of the peroxiredoxin family of peroxidases. It belongs to the peroxiredoxin 2-Cys subgroup containing three cysteines at positions 47, 66, and 168. The cloning and overexpression in Escherichia coli of recombinant wild type SP-22 and its three cysteine mutants (C47S, C66S, and C168S) are reported. Purified His-tagged SP-22 was fully active with Cys-47 being confirmed as the catalytic residue. The enzyme forms a stable decameric toroid consisting of five basic dimeric units containing intermolecular disulfide bonds linking the catalytically active Cys-47 of one subunit and Cys-168 of the adjacent monomer. The disulfide bonds are not required for overall structural integrity. The toroidal units have average external and internal diameters of 15 and 7 nm, respectively, and can form stacks in a lateral arrangement of two or three rings. C47S had a pronounced tendency to stack in long tubular structures containing up to 60 rings. Further unusual structural features are the presence of radial spikes projecting from the external surface and ordered electron-dense material within the central cavity of the toroid.
Journal of Biological Chemistry | 2002
James Reid; Sharon M. Kelly; Kate Watt; Nicholas C. Price; Iain J. McEwan
Journal of Biological Chemistry | 2003
Antonio Garofalo; Marie-Claire Rowlinson; Ngwa A. Amambua; Jacqueline M. Hughes; Sharon M. Kelly; Nicholas C. Price; Alan Cooper; David G. Watson; Malcolm W. Kennedy; Janette E. Bradley
Journal of Molecular Biology | 1999
Paul J. Hurd; Alan J. Whitmarsh; Geoffrey S. Baldwin; Sharon M. Kelly; Jonathan P. Waltho; Nicholas C. Price; Bernard Connolly; David P. Hornby
Journal of Biological Chemistry | 2003
M. Ines Borges-Walmsley; Jeremy Beauchamp; Sharon M. Kelly; Kornelia Jumel; Denise Candlish; Stephen E. Harding; Nicholas C. Price; Adrian R. Walmsley
Archive | 2009
Nicholas C. Price; Jacqueline Nairn
Methods of Molecular Biology | 1999
Andrew W. Munro; Sharon M. Kelly; Nicholas C. Price
Archive | 2010
Katharina Fischer; Sharon M. Kelly; Kate Watt; Nicholas C. Price; Iain J. McEwan