1hw1: Difference between revisions

Revision as of 08:54, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1hw1.png

Template:STRUCTURE 1hw1

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

Template:ABSTRACT PUBMED 11279025

About this StructureAbout this Structure

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

ReferenceReference

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

Page seeded by OCA on Tue Jul 1 08:54:14 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1hw1.jpg|left|200px]]
+{{Seed}}
+[[Image:1hw1.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1hw1|  PDB=1hw1  |  SCENE=  }}
-'''THE FADR-DNA COMPLEX: TRANSCRIPTIONAL CONTROL OF FATTY ACID METABOLISM IN ESCHERICHIA COLI'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11279025}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11279025 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11279025}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Helix bundle]]
 [[Category: Helix-turn-helix]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:17:15 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 08:54:14 2008''