2asy

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|ACTIVITY=
|ACTIVITY=
|GENE= ydhR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|GENE= ydhR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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|RELATEDENTRY=[[1wd6|1WD6]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2asy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2asy OCA], [http://www.ebi.ac.uk/pdbsum/2asy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2asy RCSB]</span>
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[[Category: structural genomic]]
[[Category: structural genomic]]
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Revision as of 22:56, 30 March 2008


PDB ID 2asy

Drag the structure with the mouse to rotate
Gene: ydhR (Escherichia coli)
Related: 1WD6


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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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