1yhd

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(New page: 200px<br /><applet load="1yhd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yhd" /> '''The solution structure of YGGX from Escheric...)
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'''The solution structure of YGGX from Escherichia Coli'''<br />
'''The solution structure of YGGX from Escherichia Coli'''<br />
==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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1YHD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YHD OCA].
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1YHD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YHD OCA].
==Reference==
==Reference==
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[[Category: Gehring, K.]]
[[Category: Gehring, K.]]
[[Category: Landgraf, D.]]
[[Category: Landgraf, D.]]
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[[Category: Osborne, M.J.]]
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[[Category: Osborne, M J.]]
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[[Category: Pomposiello, P.J.]]
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[[Category: Pomposiello, P J.]]
[[Category: Siddiqui, N.]]
[[Category: Siddiqui, N.]]
[[Category: helix bundle]]
[[Category: helix bundle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:05:21 2008''

Revision as of 14:05, 21 February 2008


1yhd

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The solution structure of YGGX from Escherichia Coli

Overview

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.

About this Structure

1YHD is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The solution structure of the oxidative stress-related protein YggX from Escherichia coli., Osborne MJ, Siddiqui N, Landgraf D, Pomposiello PJ, Gehring K, Protein Sci. 2005 Jun;14(6):1673-8. Epub 2005 May 9. PMID:15883188

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