|Protein Science (2005) 14(12):3115-20|
|Northeast Structural Genomics Consortium|
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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.
|metabolism chemistry enzymology |
|Binding Sites Protein Structure, Tertiary Amino Acid Sequence Models, Molecular Molecular Sequence Data Escherichia coli Escherichia coli Proteins Mixed Function Oxygenases Sequence Alignment Protein Structure, Quaternary Sequence Homology, Amino Acid Nuclear Magnetic Resonance, Biomolecular |
|4 (Last update: 03/16/2019 8:23:55pm)|
|Protein Sci. 2005 Dec;14(12):3115-20. Epub 2005 Oct 31.|