2oxl
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(New page: 200px<br /><applet load="2oxl" size="350" color="white" frame="true" align="right" spinBox="true" caption="2oxl, resolution 1.80Å" /> '''Structure and Functi...)
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Revision as of 10:36, 23 January 2008
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Structure and Function of the E. coli Protein YmgB: a Protein Critical for Biofilm Formation and Acid Resistance
Overview
The Escherichia coli gene cluster ymgABC was identified in transcriptome, studies to have a role in biofilm development and stability. In this, study, we showed that YmgB represses biofilm formation in rich medium, containing glucose, decreases cellular motility, and protects the cell, from acid indicating that YmgB has a major role in acid-resistance in E., coli. Our data show that these phenotypes are potentially mediated through, interactions with the important cell signal indole. In addition, gel, mobility-shift assays suggest that YmgB may be a non-specific DNA-binding, protein. Using nickel-enrichment DNA microarrays, we showed that YmgB, binds, either directly or indirectly, via a probable ligand, genes, important for biofilm formation. To advance our understanding of the, function of YmgB, we used X-ray crystallography to solve the structure of, the protein to 1.8 A resolution. YmgB is a biological dimer that is, structurally homologous to the E. coli gene regulatory protein Hha, despite having only 5% sequence identity. This supports our DNA microarray, data showing that YmgB is a gene regulatory protein. Therefore, this, protein, which clearly has a critical role in acid-resistance in E. coli, has been renamed as AriR for regulator of acid resistance influenced by, indole.
About this Structure
2OXL is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
Reference
Structure and function of the Escherichia coli protein YmgB: a protein critical for biofilm formation and acid-resistance., Lee J, Page R, Garcia-Contreras R, Palermino JM, Zhang XS, Doshi O, Wood TK, Peti W, J Mol Biol. 2007 Oct 12;373(1):11-26. Epub 2007 Aug 2. PMID:17765265
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