2hgv: Difference between revisions

Revision as of 03:47, 29 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:2hgv.png

Template:STRUCTURE 2hgv

N-terminal GAF domain of transcriptional pleiotropic repressor CodYN-terminal GAF domain of transcriptional pleiotropic repressor CodY

Template:ABSTRACT PUBMED 16488888

About this StructureAbout this Structure

2HGV is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

ReferenceReference

The structure of CodY, a GTP- and isoleucine-responsive regulator of stationary phase and virulence in gram-positive bacteria., Levdikov VM, Blagova E, Joseph P, Sonenshein AL, Wilkinson AJ, J Biol Chem. 2006 Apr 21;281(16):11366-73. Epub 2006 Feb 17. PMID:16488888

Crystallization of the GTP-dependent transcriptional regulator CodY from Bacillus subtilis., Blagova EV, Levdikov VM, Tachikawa K, Sonenshein AL, Wilkinson AJ, Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):155-7. Epub 2002, Dec 19. PMID:12499555

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OCA

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-[[Image:2hgv.gif|left|200px]]
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 {{STRUCTURE_2hgv|  PDB=2hgv  |  SCENE=  }}
-'''N-terminal GAF domain of transcriptional pleiotropic repressor CodY'''
+===N-terminal GAF domain of transcriptional pleiotropic repressor CodY===
-==Overview==
+<!--
-CodY is a global regulator of transcription in gram-positive bacteria. It represses during growth genes required for adaptation to nutrient limitation, including virulence genes in some human pathogens. CodY activity is regulated by GTP and branched chain amino acids, metabolites whose intracellular concentrations drop as cells enter stationary phase. Although CodY has a highly conserved sequence, it has no significant similarity to proteins of known structure. Here we report crystal structures of two fragments of CodY from Bacillus subtilis that clearly constitute its cofactor and DNA binding domains and reveal that CodY is a chimera of previously observed folding units. The N-terminal cofactor-binding fragment adopts a fold reminiscent of the GAF domains found in cyclic nucleotide phosphodiesterases and adenylate cyclases. It is a dimer stabilized by an intermolecular six alpha-helical bundle that buries an extensive apolar surface rich in residues invariant in CodY orthologues. The branched chain amino acid ligands reside in hydrophobic pockets of each monomer distal to the dimer-forming surface. The structure of the C-terminal DNA binding domain belongs to the winged helix-turn-helix family. The implications of the structure for DNA binding by CodY and its control by cofactor binding are discussed.
+The line below this paragraph, {{ABSTRACT_PUBMED_16488888}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16488888 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16488888}}
 ==About this Structure==
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 ==Reference==
 The structure of CodY, a GTP- and isoleucine-responsive regulator of stationary phase and virulence in gram-positive bacteria., Levdikov VM, Blagova E, Joseph P, Sonenshein AL, Wilkinson AJ, J Biol Chem. 2006 Apr 21;281(16):11366-73. Epub 2006 Feb 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16488888 16488888]
+Crystallization of the GTP-dependent transcriptional regulator CodY from Bacillus subtilis., Blagova EV, Levdikov VM, Tachikawa K, Sonenshein AL, Wilkinson AJ, Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):155-7. Epub 2002, Dec 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12499555 12499555]
 [[Category: Bacillus subtilis]]
 [[Category: Single protein]]
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 [[Category: Repressor]]
 [[Category: Transcription regulation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 06:16:44 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:47:31 2008''