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1YHD

The solution structure of YGGX from Escherichia Coli

Summary for 1YHD
Entry DOI10.2210/pdb1yhd/pdb
DescriptorUPF0269 protein yggX (1 entity in total)
Functional Keywordshelix bundle, unknown function
Biological sourceEscherichia coli
Total number of polymer chains1
Total formula weight12096.74
Authors
Osborne, M.J.,Siddiqui, N.,Landgraf, D.,Pomposiello, P.J.,Gehring, K. (deposition date: 2005-01-07, release date: 2005-01-18, Last modification date: 2024-05-22)
Primary citationOsborne, M.J.,Siddiqui, N.,Landgraf, D.,Pomposiello, P.J.,Gehring, K.
The solution structure of the oxidative stress-related protein YggX from Escherichia coli.
Protein Sci., 14:1673-1678, 2005
Cited by
PubMed Abstract: 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 beta-sheets and three alpha-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.
PubMed: 15883188
DOI: 10.1110/ps.051358105
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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