2asy
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(New page: 200px<br /><applet load="2asy" size="450" color="white" frame="true" align="right" spinBox="true" caption="2asy" /> '''Solution Structure of ydhR protein from Esch...)
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Revision as of 06:13, 21 November 2007
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Solution Structure of ydhR protein from Escherichia coli
Overview
YdhR is a 101-residue conserved protein from Escherichia coli. Sequence, searches reveal that the protein has >50% identity to proteins found in a, variety of other bacterial genomes. Using size exclusion chromatography, and fluorescence spectroscopy, we determined that ydhR exists in a dimeric, state with a dissociation constant of approximately 40 nM. The, three-dimensional structure of dimeric ydhR was determined using NMR, spectroscopy. A total of 3400 unambiguous NOEs, both manually and, automatically assigned, were used for the structure calculation that was, refined using an explicit hydration shell. A family of 20 structures was, obtained with a backbone RMSD of 0.48 A for elements of secondary, structure. The structure reveals a dimeric alpha,beta fold characteristic, of the alpha+beta barrel superfamily of proteins. Bioinformatic approaches, were used to show that ydhR likely belongs to a recently identified group, of mono-oxygenase proteins that includes ActVA-Orf6 and YgiN and are, involved in the oxygenation of polyaromatic ring compounds.
About this Structure
2ASY is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Solution structure of the Escherichia coli protein ydhR: a putative mono-oxygenase., Revington M, Semesi A, Yee A, Shaw GS, Protein Sci. 2005 Dec;14(12):3115-20. Epub 2005 Oct 31. PMID:16260765
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