<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1yhd ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
Revision as of 18:38, 7 February 2016
The solution structure of YGGX from Escherichia Coli
[FETP_ECOLI] Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes. Necessary to maintain high levels of aconitase under oxidative stress.[1][2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑Pomposiello PJ, Koutsolioutsou A, Carrasco D, Demple B. SoxRS-regulated expression and genetic analysis of the yggX gene of Escherichia coli. J Bacteriol. 2003 Nov;185(22):6624-32. PMID:14594836
↑Osborne MJ, Siddiqui N, Landgraf D, Pomposiello PJ, Gehring K. The solution structure of the oxidative stress-related protein YggX from Escherichia coli. Protein Sci. 2005 Jun;14(6):1673-8. Epub 2005 May 9. PMID:15883188 doi:10.1110/ps.051358105
↑Osborne MJ, Siddiqui N, Landgraf D, Pomposiello PJ, Gehring K. The solution structure of the oxidative stress-related protein YggX from Escherichia coli. Protein Sci. 2005 Jun;14(6):1673-8. Epub 2005 May 9. PMID:15883188 doi:10.1110/ps.051358105
