Literature DB >> 23338727

The zinc-binding fragment of HypA from Helicobacter pylori: a tempting site also for nickel ions.

Magdalena Rowinska-Zyrek1, Slawomir Potocki, Danuta Witkowska, Daniela Valensin, Henryk Kozlowski.   

Abstract

HypA, a nickel accessory protein from H. pylori, binds a zinc ion in it's structural site, a loop with two conserved CXXC motifs (Ac-ELECKDCSHVFKPNALDYGVCEKCHS-NH(2)). There are at least three hypotheses on the binding mode of this ion. In this paper, we try to understand how Zn(2+) binds to this fragment and why Ni(2+), a metal with quite a high affinity towards thiolic sites, doesn't compete with zinc in the binding to this motif. Potentiometric titrations, mass spectrometry, NMR, UV-Vis and CD spectroscopy help us to compare the coordination modes in both metal complexes and discuss their thermodynamic stabilities.

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Year:  2013        PMID: 23338727     DOI: 10.1039/c2dt32195e

Source DB:  PubMed          Journal:  Dalton Trans        ISSN: 1477-9226            Impact factor:   4.390


  3 in total

Review 1.  Nickel trafficking system responsible for urease maturation in Helicobacter pylori.

Authors:  Rui-Guang Ge; Dong-Xian Wang; Ming-Cong Hao; Xue-Song Sun
Journal:  World J Gastroenterol       Date:  2013-12-07       Impact factor: 5.742

2.  Metal Binding Ability of Small Peptides Containing Cysteine Residues.

Authors:  Márton Lukács; Dóra Csilla Pálinkás; Györgyi Szunyog; Katalin Várnagy
Journal:  ChemistryOpen       Date:  2021-04       Impact factor: 2.630

3.  Histidine tracts in human transcription factors: insight into metal ion coordination ability.

Authors:  Aleksandra Hecel; Joanna Wątły; Magdalena Rowińska-Żyrek; Jolanta Świątek-Kozłowska; Henryk Kozłowski
Journal:  J Biol Inorg Chem       Date:  2017-12-07       Impact factor: 3.358

  3 in total

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