1sd5

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(New page: 200px<br /><applet load="1sd5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sd5, resolution 1.68&Aring;" /> '''Crystal structure of...)
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[[Image:1sd5.gif|left|200px]]<br /><applet load="1sd5" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1sd5.gif|left|200px]]<br /><applet load="1sd5" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1sd5, resolution 1.68&Aring;" />
caption="1sd5, resolution 1.68&Aring;" />
'''Crystal structure of Rv1626'''<br />
'''Crystal structure of Rv1626'''<br />
==Overview==
==Overview==
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We describe the crystal structure of Rv1626 from Mycobacterium, tuberculosis at 1.48 A resolution and the corresponding solution structure, determined from small angle X-ray scattering. The N-terminal domain shows, structural homology to the receiver domains found in bacterial, two-component systems. The C-terminal domain has high structural homology, to a recently discovered RNA binding domain involved in transcriptional, antitermination. The molecule in solution was found to be monomeric as it, is in the crystal, but in solution it undergoes a conformational change, that is triggered by changes in ionic strength. This is the first, structure that links the phosphorylation cascade of the two-component, systems with the antitermination event in the transcriptional machinery., Rv1626 belongs to a family of proteins, which we propose calling, phosphorylation-dependent transcriptional antitermination regulators, so, far only found in bacteria, and includes NasT, a protein from the, assimilatory nitrate/nitrite reductase operon of Azetobacter vinelandii.
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We describe the crystal structure of Rv1626 from Mycobacterium tuberculosis at 1.48 A resolution and the corresponding solution structure determined from small angle X-ray scattering. The N-terminal domain shows structural homology to the receiver domains found in bacterial two-component systems. The C-terminal domain has high structural homology to a recently discovered RNA binding domain involved in transcriptional antitermination. The molecule in solution was found to be monomeric as it is in the crystal, but in solution it undergoes a conformational change that is triggered by changes in ionic strength. This is the first structure that links the phosphorylation cascade of the two-component systems with the antitermination event in the transcriptional machinery. Rv1626 belongs to a family of proteins, which we propose calling phosphorylation-dependent transcriptional antitermination regulators, so far only found in bacteria, and includes NasT, a protein from the assimilatory nitrate/nitrite reductase operon of Azetobacter vinelandii.
==About this Structure==
==About this Structure==
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1SD5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_h37rv Mycobacterium tuberculosis h37rv] with IOD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SD5 OCA].
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1SD5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_h37rv Mycobacterium tuberculosis h37rv] with <scene name='pdbligand=IOD:'>IOD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SD5 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Feng, V.]]
[[Category: Feng, V.]]
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[[Category: Morth, J.P.]]
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[[Category: Morth, J P.]]
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[[Category: Perry, L.J.]]
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[[Category: Perry, L J.]]
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[[Category: Svergun, D.I.]]
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[[Category: Svergun, D I.]]
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[[Category: TBSGC, TB.Structural.Genomics.Consortium.]]
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[[Category: TBSGC, TB Structural Genomics Consortium.]]
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[[Category: Tucker, P.A.]]
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[[Category: Tucker, P A.]]
[[Category: IOD]]
[[Category: IOD]]
[[Category: antiterminator]]
[[Category: antiterminator]]
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[[Category: two components system]]
[[Category: two components system]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:17:38 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:00:15 2008''

Revision as of 13:00, 21 February 2008


1sd5, resolution 1.68Å

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Crystal structure of Rv1626

Overview

We describe the crystal structure of Rv1626 from Mycobacterium tuberculosis at 1.48 A resolution and the corresponding solution structure determined from small angle X-ray scattering. The N-terminal domain shows structural homology to the receiver domains found in bacterial two-component systems. The C-terminal domain has high structural homology to a recently discovered RNA binding domain involved in transcriptional antitermination. The molecule in solution was found to be monomeric as it is in the crystal, but in solution it undergoes a conformational change that is triggered by changes in ionic strength. This is the first structure that links the phosphorylation cascade of the two-component systems with the antitermination event in the transcriptional machinery. Rv1626 belongs to a family of proteins, which we propose calling phosphorylation-dependent transcriptional antitermination regulators, so far only found in bacteria, and includes NasT, a protein from the assimilatory nitrate/nitrite reductase operon of Azetobacter vinelandii.

About this Structure

1SD5 is a Single protein structure of sequence from Mycobacterium tuberculosis h37rv with as ligand. Full crystallographic information is available from OCA.

Reference

The crystal and solution structure of a putative transcriptional antiterminator from Mycobacterium tuberculosis., Morth JP, Feng V, Perry LJ, Svergun DI, Tucker PA, Structure. 2004 Sep;12(9):1595-605. PMID:15341725

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