Structure of a Nickel Chaperone, HypA, from Helicobacter pylon Reveals Two Distinct Metal Binding Sites.
Metaltochaperones bind metals and ensure the safe delivery of metals to the targets. They are required for the activation and maturation of nickel-containing enzymes [Ni,Fe]-hydrogenase and urease. Metallochaperone HypA was found to be essential to facilitate nickel delivery to hydrogenase together...
| Publicado en: | Journal of the American Chemical Society Vol. 131; no. 29; pp. 10031 - 10041 |
|---|---|
| Autores principales: | , , , |
| Formato: | Artículo |
| Publicado: |
American Chemical Society
7/29/2009
|
| Materias: | |
| Acceso en línea: | Ver este registro en EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=hlh&AN=43797141&site=ehost-live header: @attributes: shortDbName: hlh uiTerm: 43797141 longDbName: Humanities International Complete uiTag: AN controlInfo: bkinfo: jinfo: jid: 00027863 ACS jtl: Journal of the American Chemical Society issn: 00027863 maglogo: N pubinfo: dt: 7/29/2009 vid: 131 iid: 29 pid: 997 pub: American Chemical Society artinfo: ui: 43797141 10.1021/ja900543y ppf: 10031 ppct: 10 formats: tig: atl: Structure of a Nickel Chaperone, HypA, from Helicobacter pylon Reveals Two Distinct Metal Binding Sites. aug: au: Xia, Wei Li, Hongyan Sze, Kong-Hung Sun, Hongzhe affil: Department of Chemistry and Open Laboratory of Chemical Biology, University of Hong Kong, Pokfulam, Hong Kong, People's Republic of China su: Molecular chaperones Nickel compounds Metal bonding Binding sites Helicobacter pylori Zinc compounds Nuclear magnetic resonance spectroscopy Cysteine proteinases sug: subj: Molecular chaperones Nickel compounds Metal bonding Binding sites Helicobacter pylori Zinc compounds Nuclear magnetic resonance spectroscopy Cysteine proteinases ab: Metaltochaperones bind metals and ensure the safe delivery of metals to the targets. They are required for the activation and maturation of nickel-containing enzymes [Ni,Fe]-hydrogenase and urease. Metallochaperone HypA was found to be essential to facilitate nickel delivery to hydrogenase together with its partner HypB, although the detailed mechanism is not clear. In this study, we have cloned hypA gene from Helicobacterpylori (strain 26695), overexpressed, and purified the protein. The zinc-bound HypA (Zn-HypA) exists as a monomer in solution, and its solution structure was determined by NMA spectroscopy together with molecular dynamics simulated annealing. Zn-HypA folds into two domains, including a zinc domain and a nickel domain with a mixed α/β structure. The former houses a rigid zinc-binding site possibly with the role of structural stabilization, whereas the latter harbors a nickel-binding site at the N-terminus. Zinc binds to the four conserved cysteines tetrahedrally as evidenced by Cd NMR spectroscopy, and nickel coordinates with four nitrogens of the protein probably in a square-planar geometry. Low coordination number of Ni may allow the metal to be readily transferred to its downstream receptors. Our studies may shed light on how the metallochaperone exerts its functions in intracellular nickel delivery. pubtype: Academic Journal doctype: Article src: R language: English refInfo: copyright: @attributes: flag: Y dt: @attributes: year: 2009 holdings: @attributes: islocal: N |
|---|