1h9r

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[[Image:1h9r.jpg|left|200px]]<br /><applet load="1h9r" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1h9r.jpg|left|200px]]
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caption="1h9r, resolution 1.9&Aring;" />
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'''TUNGSTATE BOUND COMPLEX DIMOP DOMAIN OF MODE FROM E.COLI'''<br />
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{{Structure
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|PDB= 1h9r |SIZE=350|CAPTION= <scene name='initialview01'>1h9r</scene>, resolution 1.9&Aring;
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|SITE= <scene name='pdbsite=AC1:Wo4+Binding+Site+For+Residue+B1262'>AC1</scene>, <scene name='pdbsite=AC2:Wo4+Binding+Site+For+Residue+A1262'>AC2</scene> and <scene name='pdbsite=AC3:Ni+Binding+Site+For+Resdiue+B1263'>AC3</scene>
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|LIGAND= <scene name='pdbligand=WO4:TUNGSTATE(VI)ION'>WO4</scene> and <scene name='pdbligand=NI:NICKEL (II) ION'>NI</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''TUNGSTATE BOUND COMPLEX DIMOP DOMAIN OF MODE FROM E.COLI'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1H9R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=WO4:'>WO4</scene> and <scene name='pdbligand=NI:'>NI</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Wo4+Binding+Site+For+Residue+B1262'>AC1</scene>, <scene name='pdbsite=AC2:Wo4+Binding+Site+For+Residue+A1262'>AC2</scene> and <scene name='pdbsite=AC3:Ni+Binding+Site+For+Resdiue+B1263'>AC3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H9R OCA].
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1H9R is a [[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=1H9R OCA].
==Reference==
==Reference==
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Oxyanion binding alters conformation and quaternary structure of the c-terminal domain of the transcriptional regulator mode. Implications for molybdate-dependent regulation, signaling, storage, and transport., Gourley DG, Schuttelkopf AW, Anderson LA, Price NC, Boxer DH, Hunter WN, J Biol Chem. 2001 Jun 8;276(23):20641-7. Epub 2001 Mar 20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11259434 11259434]
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Oxyanion binding alters conformation and quaternary structure of the c-terminal domain of the transcriptional regulator mode. Implications for molybdate-dependent regulation, signaling, storage, and transport., Gourley DG, Schuttelkopf AW, Anderson LA, Price NC, Boxer DH, Hunter WN, J Biol Chem. 2001 Jun 8;276(23):20641-7. Epub 2001 Mar 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11259434 11259434]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: transcription regulator]]
[[Category: transcription regulator]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:59:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:34:12 2008''

Revision as of 09:34, 20 March 2008


PDB ID 1h9r

Drag the structure with the mouse to rotate
, resolution 1.9Å
Sites: , and
Ligands: and
Coordinates: save as pdb, mmCIF, xml



TUNGSTATE BOUND COMPLEX DIMOP DOMAIN OF MODE FROM E.COLI


Overview

The molybdate-dependent transcriptional regulator ModE of Escherichia coli functions as a sensor of intracellular molybdate concentration and a regulator for the transcription of several operons that control the uptake and utilization of molybdenum. We present two high-resolution crystal structures of the C-terminal oxyanion-binding domain in complex with molybdate and tungstate. The ligands bind between subunits at the dimerization interface, and analysis reveals that oxyanion selectivity is determined primarily by size. The relevance of the structures is indicated by fluorescence measurements, which show that the oxyanion binding properties of the C-terminal domain of ModE are similar to those of the full-length protein. Comparisons with the apoprotein structure have identified structural rearrangements that occur on binding oxyanion. This molybdate-dependent conformational switch promotes a change in shape and alterations to the surface of the protein and may provide the signal for recruitment of other proteins to construct the machinery for transcription. Sequence and structure-based comparisons lead to a classification of molybdate-binding proteins.

About this Structure

1H9R is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Oxyanion binding alters conformation and quaternary structure of the c-terminal domain of the transcriptional regulator mode. Implications for molybdate-dependent regulation, signaling, storage, and transport., Gourley DG, Schuttelkopf AW, Anderson LA, Price NC, Boxer DH, Hunter WN, J Biol Chem. 2001 Jun 8;276(23):20641-7. Epub 2001 Mar 20. PMID:11259434

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