1hw1

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[[Image:1hw1.jpg|left|200px]]<br /><applet load="1hw1" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1hw1.jpg|left|200px]]
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caption="1hw1, resolution 1.5&Aring;" />
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'''THE FADR-DNA COMPLEX: TRANSCRIPTIONAL CONTROL OF FATTY ACID METABOLISM IN ESCHERICHIA COLI'''<br />
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{{Structure
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|PDB= 1hw1 |SIZE=350|CAPTION= <scene name='initialview01'>1hw1</scene>, resolution 1.5&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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|ACTIVITY=
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|GENE= FADR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''THE FADR-DNA COMPLEX: TRANSCRIPTIONAL CONTROL OF FATTY ACID METABOLISM IN ESCHERICHIA COLI'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1HW1 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=SO4:'>SO4</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HW1 OCA].
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1HW1 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=1HW1 OCA].
==Reference==
==Reference==
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The FadR.DNA complex. Transcriptional control of fatty acid metabolism in Escherichia coli., Xu Y, Heath RJ, Li Z, Rock CO, White SW, J Biol Chem. 2001 May 18;276(20):17373-9. Epub 2001 Feb 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11279025 11279025]
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The FadR.DNA complex. Transcriptional control of fatty acid metabolism in Escherichia coli., Xu Y, Heath RJ, Li Z, Rock CO, White SW, J Biol Chem. 2001 May 18;276(20):17373-9. Epub 2001 Feb 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11279025 11279025]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: helix-turn-helix]]
[[Category: helix-turn-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:05:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:42:17 2008''

Revision as of 09:42, 20 March 2008


PDB ID 1hw1

Drag the structure with the mouse to rotate
, resolution 1.5Å
Ligands: and
Gene: FADR (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



THE FADR-DNA COMPLEX: TRANSCRIPTIONAL CONTROL OF FATTY ACID METABOLISM IN ESCHERICHIA COLI


Overview

In Escherichia coli, the expression of fatty acid metabolic genes is controlled by the transcription factor, FadR. The affinity of FadR for DNA is controlled by long chain acyl-CoA molecules, which bind to the protein and modulate gene expression. The crystal structure of FadR reveals a two domain dimeric molecule where the N-terminal domains bind DNA, and the C-terminal domains bind acyl-CoA. The DNA binding domain has a winged-helix motif, and the C-terminal domain resembles the sensor domain of the Tet repressor. The FadR.DNA complex reveals how the protein interacts with DNA and specifically recognizes a palindromic sequence. Structural and functional similarities to the Tet repressor and the BmrR transcription factors suggest how the binding of the acyl-CoA effector molecule to the C-terminal domain may affect the DNA binding affinity of the N-terminal domain. We suggest that the binding of acyl-CoA disrupts a buried network of charged and polar residues in the C-terminal domain, and the resulting conformational change is transmitted to the N-terminal domain via a domain-spanning alpha-helix.

About this Structure

1HW1 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The FadR.DNA complex. Transcriptional control of fatty acid metabolism in Escherichia coli., Xu Y, Heath RJ, Li Z, Rock CO, White SW, J Biol Chem. 2001 May 18;276(20):17373-9. Epub 2001 Feb 13. PMID:11279025

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