2vbw

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[[Image:2vbw.jpg|left|200px]]<br /><applet load="2vbw" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2vbw.jpg|left|200px]]
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caption="2vbw, resolution 2.20&Aring;" />
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'''FEAST OR FAMINE REGULATORY PROTEIN (RV3291C)FROM M. TUBERCULOSIS COMPLEXED WITH L-PHENYLALANINE'''<br />
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{{Structure
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|PDB= 2vbw |SIZE=350|CAPTION= <scene name='initialview01'>2vbw</scene>, resolution 2.20&Aring;
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|SITE= <scene name='pdbsite=AC1:PHE+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''FEAST OR FAMINE REGULATORY PROTEIN (RV3291C)FROM M. TUBERCULOSIS COMPLEXED WITH L-PHENYLALANINE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2VBW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=PHE:'>PHE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:PHE+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VBW OCA].
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2VBW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VBW OCA].
==Reference==
==Reference==
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Mechanistic insights from the crystal structures of a feast/famine regulatory protein from Mycobacterium tuberculosis H37Rv., Shrivastava T, Ramachandran R, Nucleic Acids Res. 2007;35(21):7324-35. Epub 2007 Oct 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17962306 17962306]
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Mechanistic insights from the crystal structures of a feast/famine regulatory protein from Mycobacterium tuberculosis H37Rv., Shrivastava T, Ramachandran R, Nucleic Acids Res. 2007;35(21):7324-35. Epub 2007 Oct 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17962306 17962306]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
[[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 18:55:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:45:17 2008''

Revision as of 16:45, 20 March 2008


PDB ID 2vbw

Drag the structure with the mouse to rotate
, resolution 2.20Å
Sites:
Ligands:
Coordinates: save as pdb, mmCIF, xml



FEAST OR FAMINE REGULATORY PROTEIN (RV3291C)FROM M. TUBERCULOSIS COMPLEXED WITH L-PHENYLALANINE


Overview

Rv3291c gene from Mycobacterium tuberculosis codes for a transcriptional regulator belonging to the (leucine responsive regulatory protein/regulator of asparigine synthase C gene product) Lrp/AsnC-family. We have identified a novel effector-binding site from crystal structures of the apo protein, complexes with a variety of amino acid effectors, X-ray based ligand screening and qualitative fluorescence spectroscopy experiments. The new effector site is in addition to the structural characterization of another distinct site in the protein conserved in the related AsnC-family of regulators. The structures reveal that the ligand-binding loops of two crystallographically independent subunits adopt different conformations to generate two distinct effector-binding sites. A change in the conformation of the binding site loop 100-106 in the B subunit is apparently necessary for octameric association and also allows the loop to interact with a bound ligand in the newly identified effector-binding site. There are four sites of each kind in the octamer and the protein preferentially binds to aromatic amino acids. While amino acids like Phe, Tyr and Trp exhibit binding to only one site, His exhibits binding to both sites. Binding of Phe is accompanied by a conformational change of 3.7 A in the 75-83 loop, which is advantageously positioned to control formation of higher oligomers. Taken together, the present studies suggest an elegant control mechanism for global transcription regulation involving binding of ligands to the two sites, individually or collectively.

About this Structure

2VBW is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Mechanistic insights from the crystal structures of a feast/famine regulatory protein from Mycobacterium tuberculosis H37Rv., Shrivastava T, Ramachandran R, Nucleic Acids Res. 2007;35(21):7324-35. Epub 2007 Oct 25. PMID:17962306

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