2jhe

From Proteopedia

(Difference between revisions)

Current revision

N-terminal domain of TyrR transcription factor (residues 1 - 190)

Structural highlights

2jhe is a 4 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TYRR_ECOLI Involved in transcriptional regulation of aromatic amino acid biosynthesis and transport. Modulates the expression of at least 8 unlinked operons. Seven of these operons are regulated in response to changes in the concentration of the three aromatic amino acids (phenylalanine, tyrosine and tryptophan). These amino acids are suggested to act as co-effectors which bind to the TyrR protein to form an active regulatory protein. In most cases TyrR causes negative regulation, but positive effects on the tyrP gene have been observed at high phenylalanine concentrations.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The X-ray structure of the N-terminal domain of TyrR has been solved to a resolution of 2.3 A. It reveals a modular protein containing an ACT domain, a connecting helix, a PAS domain and a C-terminal helix. Two dimers are present in the asymmetric unit with one monomer of each pair exhibiting a large rigid-body movement that results in a hinging around residue 74 of approximately 50 degrees . The structure of the dimer is discussed with reference to other transcription regulator proteins. Putative binding sites are identified for the aromatic amino acid cofactors.

Crystal structure of the N-terminal domain of the TyrR transcription factor responsible for gene regulation of aromatic amino acid biosynthesis and transport in Escherichia coli K12.,Verger D, Carr PD, Kwok T, Ollis DL J Mol Biol. 2007 Mar 16;367(1):102-12. Epub 2006 Dec 12. PMID:17222426^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Verger D, Carr PD, Kwok T, Ollis DL. Crystal structure of the N-terminal domain of the TyrR transcription factor responsible for gene regulation of aromatic amino acid biosynthesis and transport in Escherichia coli K12. J Mol Biol. 2007 Mar 16;367(1):102-12. Epub 2006 Dec 12. PMID:17222426 doi:10.1016/j.jmb.2006.12.018

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2jhe"

@@ Line 3: / Line 3: @@
 <StructureSection load='2jhe' size='340' side='right'caption='[[2jhe]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2jhe]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JHE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2jhe]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JHE FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AE3:2-(2-ETHOXYETHOXY)ETHANOL'>AE3</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AE3:2-(2-ETHOXYETHOXY)ETHANOL'>AE3</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jhe OCA], [https://pdbe.org/2jhe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jhe RCSB], [https://www.ebi.ac.uk/pdbsum/2jhe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jhe ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/TYRR_ECOLI TYRR_ECOLI]] Involved in transcriptional regulation of aromatic amino acid biosynthesis and transport. Modulates the expression of at least 8 unlinked operons. Seven of these operons are regulated in response to changes in the concentration of the three aromatic amino acids (phenylalanine, tyrosine and tryptophan). These amino acids are suggested to act as co-effectors which bind to the TyrR protein to form an active regulatory protein. In most cases TyrR causes negative regulation, but positive effects on the tyrP gene have been observed at high phenylalanine concentrations.
+[https://www.uniprot.org/uniprot/TYRR_ECOLI TYRR_ECOLI] Involved in transcriptional regulation of aromatic amino acid biosynthesis and transport. Modulates the expression of at least 8 unlinked operons. Seven of these operons are regulated in response to changes in the concentration of the three aromatic amino acids (phenylalanine, tyrosine and tryptophan). These amino acids are suggested to act as co-effectors which bind to the TyrR protein to form an active regulatory protein. In most cases TyrR causes negative regulation, but positive effects on the tyrP gene have been observed at high phenylalanine concentrations.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Ecoli]]
+[[Category: Escherichia coli K-12]]
 [[Category: Large Structures]]
-[[Category: Carr, P D]]
+[[Category: Carr PD]]
-[[Category: Kwok, T]]
+[[Category: Kwok T]]
-[[Category: Ollis, D L]]
+[[Category: Ollis DL]]
-[[Category: Verger, D]]
+[[Category: Verger D]]
-[[Category: Activator]]
-[[Category: Aromatic hydrocarbons catabolism]]
-[[Category: Atp-binding]]
-[[Category: Dna-binding]]
-[[Category: Nucleotide-binding]]
-[[Category: Repressor]]
-[[Category: Transcription]]
-[[Category: Transcription regulation]]
-[[Category: Two-component regulatory system]]
-[[Category: Tyrr protein]]

2jhe

From Proteopedia

Current revision

N-terminal domain of TyrR transcription factor (residues 1 - 190)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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