2asy

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(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...)
Line 1: Line 1:
-
[[Image:2asy.gif|left|200px]]<br /><applet load="2asy" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2asy.gif|left|200px]]<br /><applet load="2asy" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2asy" />
caption="2asy" />
'''Solution Structure of ydhR protein from Escherichia coli'''<br />
'''Solution Structure of ydhR protein from Escherichia coli'''<br />
==Overview==
==Overview==
-
YdhR is a 101-residue conserved protein from Escherichia coli. Sequence, searches reveal that the protein has &gt;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.
+
YdhR is a 101-residue conserved protein from Escherichia coli. Sequence searches reveal that the protein has &gt;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==
==About this Structure==
-
2ASY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ASY OCA].
+
2ASY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ASY OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: OCSP, Ontario.Centre.for.Structural.Proteomics.]]
+
[[Category: OCSP, Ontario Centre for Structural Proteomics.]]
[[Category: Revington, M.]]
[[Category: Revington, M.]]
[[Category: Semesi, A.]]
[[Category: Semesi, A.]]
-
[[Category: Shaw, G.S.]]
+
[[Category: Shaw, G S.]]
[[Category: Yee, A.]]
[[Category: Yee, A.]]
[[Category: dimeric apha+beta barrel]]
[[Category: dimeric apha+beta barrel]]
Line 24: Line 24:
[[Category: structural genomics]]
[[Category: structural genomics]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:20:58 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:30:43 2008''

Revision as of 14:30, 21 February 2008


2asy

Drag the structure with the mouse to rotate

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

Page seeded by OCA on Thu Feb 21 16:30:43 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools