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The solution structure of the oxidative stress‐related protein YggX from Escherichia coli
Author(s) -
Osborne Michael J.,
Siddiqui Nadeem,
Landgraf Dirk,
Pomposiello Pablo J.,
Gehring Kalle
Publication year - 2005
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.051358105
Subject(s) - escherichia coli , antiparallel (mathematics) , protein structure , chemistry , biochemistry , oxidative stress , nuclear magnetic resonance spectroscopy , cofactor , biophysics , crystallography , biology , stereochemistry , enzyme , physics , quantum mechanics , magnetic field , gene
YggX is a highly conserved protein found only in eubacteria and is proposed to be involved in the bacterial response to oxidative stress. Here we report the solution structure of YggX from Escherichia coli determined by nuclear magnetic resonance spectroscopy. The structure of YggX displays a fold consisting of two N‐terminal antiparallel β‐sheets and three α‐helices, which shares significant structural similarity to the crystal structure of a hypothetical protein PA5148 from Pseudomonas aeruginosa . Previous studies propose YggX as an iron binding protein that is involved in cellular iron trafficking. Our data indicate that the protein alone does not bind iron in vitro, suggesting other cofactors or different conditions may be necessary for metal binding.