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ToolsHannan, Jonathan P., Whittaker, Sara B.-M., Hemmings, Andrew M., James, Richard, Kleanthous, Colin and Moore, Geoffrey R. (2000) NMR studies of metal ion binding to the Zn-finger-like HNH motif of colicin E9. Journal of Inorganic Biochemistry, 79 (1-4). pp. 365-370. ISSN 0162-0134
Full text not available from this repository. (Request a copy)Abstract
The 134 amino acid DNase domain of colicin E9 contains a zinc-finger-like HNH motif that binds divalent transition metal ions. We have used 1D 1H and 2D 1H-15N NMR methods to characterise the binding of Co2+, Ni2+ and Zn2+ to this protein. Data for the Co2+-substituted and Ni2+-substituted proteins show that the metal ion is coordinated by three histidine residues; and the NMR characteristics of the Ni2+-substituted protein show that two of the histidines are coordinated through their N(ε2) atoms and one via its N(δ1). Furthermore, the NMR spectrum of the Ni2+-substituted protein is perturbed by the presence of phosphate, consistent with an X-ray structure showing that phosphate is coordinated to bound Ni2+, and by a change in pH, consistent with an ionisable group at the metal centre with a pK(a) of 7.9. Binding of an inhibitor protein to the DNase does not perturb the resonances of the metal site, suggesting there is no substantial conformation change of the DNase HNH motif on inhibitor binding. 1H-15N NMR data for the Zn2+-substituted DNase show that this protein, like the metal-free DNase, exists as two conformers with different 1H-15N correlation NMR spectra, and that the binding of Zn2+ does not significantly perturb the spectra, and hence structures, of these conformers beyond the HNH motif region. (C) 2000 Elsevier Science Inc.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | cobalt ions,colicin,endonuclease,nickel ions,nuclear magnetic resonance spectroscopy,zinc ions,biochemistry,inorganic chemistry ,/dk/atira/pure/subjectarea/asjc/1300/1303 |
| Faculty \ School: | Faculty of Science > School of Chemistry, Pharmacy and Pharmacology Faculty of Science > School of Biological Sciences |
| UEA Research Groups: | Faculty of Science > Research Groups > Plant Sciences Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Groups > Chemistry of Life Processes Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry |
| Related URLs: | |
| Depositing User: | LivePure Connector |
| Date Deposited: | 13 Feb 2025 17:30 |
| Last Modified: | 16 Feb 2025 06:30 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/98477 |
| DOI: | 10.1016/S0162-0134(99)00235-4 |
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