1yio: Difference between revisions

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<StructureSection load='1yio' size='340' side='right'caption='[[1yio]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1yio' size='340' side='right'caption='[[1yio]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1yio]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_fluorescens_liquefaciens"_flugge_1886 "bacillus fluorescens liquefaciens" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YIO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YIO FirstGlance]. <br>
<table><tr><td colspan='2'>[[1yio]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YIO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YIO FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1yio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yio OCA], [https://pdbe.org/1yio PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yio RCSB], [https://www.ebi.ac.uk/pdbsum/1yio PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yio ProSAT]</span></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=1yio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yio OCA], [https://pdbe.org/1yio PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yio RCSB], [https://www.ebi.ac.uk/pdbsum/1yio PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yio ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O30989_PSEFL O30989_PSEFL]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1yio ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1yio ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
StyR belongs to the FixJ subfamily of signal transduction response regulators; it controls transcription of the styABCD operon coding for styrene catabolism in Pseudomonas fluorescens ST. The crystal structure of unphosphorylated StyR is reported at 2.2 A resolution. StyR is composed of an N-terminal regulatory domain (StyR-N) and a C-terminal DNA binding domain (StyR-C). The two domains are separated by an elongated linker alpha helix (34 residues), a new feature in known response regulator structures. StyR-C is structured similarly to the DNA binding domain of the response regulator NarL. StyR-N shows structural reorganization of the phosphate receiving region involved in activation/homodimerization: specific residues adopt an "active-like" conformation, and the alpha4 helix, involved in dimerization of the homologous FixJ response regulator, is trimmed to just one helical turn. Overall, structural considerations suggest that phosphorylation may act as an allosteric switch, shifting a preexisting StyR equilibrium toward the active, dimeric, DNA binding form.
An active-like structure in the unphosphorylated StyR response regulator suggests a phosphorylation- dependent allosteric activation mechanism.,Milani M, Leoni L, Rampioni G, Zennaro E, Ascenzi P, Bolognesi M Structure. 2005 Sep;13(9):1289-97. PMID:16154086<ref>PMID:16154086</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1yio" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Response regulator 3D structure|Response regulator 3D structure]]
*[[Response regulator 3D structure|Response regulator 3D structure]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus fluorescens liquefaciens flugge 1886]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ascenzi, P]]
[[Category: Pseudomonas fluorescens]]
[[Category: Bolognesi, M]]
[[Category: Ascenzi P]]
[[Category: Leoni, L]]
[[Category: Bolognesi M]]
[[Category: Milani, M]]
[[Category: Leoni L]]
[[Category: Rampioni, G]]
[[Category: Milani M]]
[[Category: Zennaro, E]]
[[Category: Rampioni G]]
[[Category: Dna binding protein]]
[[Category: Zennaro E]]
[[Category: Transcription regulation]]

Latest revision as of 13:38, 13 March 2024

Crystallographic structure of response regulator StyR from Pseudomonas fluorescens

1yio, resolution 2.20Å

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