2dg6: Difference between revisions

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[[Image:2dg6.jpg|left|200px]]


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==Crystal structure of the putative transcriptional regulator SCO5550 from Streptomyces coelicolor A3(2)==
The line below this paragraph, containing "STRUCTURE_2dg6", creates the "Structure Box" on the page.
<StructureSection load='2dg6' size='340' side='right'caption='[[2dg6]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2dg6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor_A3(2) Streptomyces coelicolor A3(2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DG6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DG6 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
{{STRUCTURE_2dg6|  PDB=2dg6  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2dg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dg6 OCA], [https://pdbe.org/2dg6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dg6 RCSB], [https://www.ebi.ac.uk/pdbsum/2dg6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dg6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O86531_STRCO O86531_STRCO]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dg/2dg6_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2dg6 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
SCO5550 from the model actinomycete Streptomyces coelicolor A3(2) was identified as a putative transcriptional regulator, and classified into the MerR family by sequence analysis. Recombined SCO5550 was successfully produced in Rhodococcus erythropolis, which can be used to stably express recombinant protein by optimizing the temperature over a wide range (4-35 degrees C). Crystal structure analysis showed that the dimerization domain (C-terminal domain) of SCO5550 has a novel fold and forms a new dimer shape, whereas the DNA-binding domain (N-terminal domain) is very similar to those of MerR family members. Such the new dimer form suggests that SCO5550 may define a new subfamily as a new member of the MerR family. Binding DNA sequence analysis of SCO5550 using the genomic systematic evolution of ligands by exponential enrichment (gSELEX) and electrophoretic mobility shift assay (EMSA) indicated that SCO5550 regulates the expression of the immediately upstream gene sco5551 encoding a putative protein, probably as a transcriptional activator.


'''Crystal structure of the putative transcriptional regulator SCO5550 from Streptomyces coelicolor A3(2)'''
Structural and genomic DNA analysis of a putative transcription factor SCO5550 from Streptomyces coelicolor A3(2): regulating the expression of gene sco5551 as a transcriptional activator with a novel dimer shape.,Hayashi T, Tanaka Y, Sakai N, Watanabe N, Tamura T, Tanaka I, Yao M Biochem Biophys Res Commun. 2013 May 24;435(1):28-33. doi:, 10.1016/j.bbrc.2013.04.017. Epub 2013 Apr 22. PMID:23618855<ref>PMID:23618855</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
==About this Structure==
</div>
2DG6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DG6 OCA].
<div class="pdbe-citations 2dg6" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
== References ==
[[Category: Streptomyces coelicolor]]
<references/>
[[Category: Hayashi, T.]]
__TOC__
[[Category: Sakai, N.]]
</StructureSection>
[[Category: Tamura, T.]]
[[Category: Large Structures]]
[[Category: Tanaka, I.]]
[[Category: Hayashi T]]
[[Category: Tanaka, Y.]]
[[Category: Sakai N]]
[[Category: Yao, M.]]
[[Category: Tamura T]]
[[Category: Merr family]]
[[Category: Tanaka I]]
[[Category: Winged-helix motif]]
[[Category: Tanaka Y]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 00:21:38 2008''
[[Category: Yao M]]

Latest revision as of 10:51, 23 October 2024

Crystal structure of the putative transcriptional regulator SCO5550 from Streptomyces coelicolor A3(2)Crystal structure of the putative transcriptional regulator SCO5550 from Streptomyces coelicolor A3(2)

Structural highlights

2dg6 is a 1 chain structure with sequence from Streptomyces coelicolor A3(2). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

O86531_STRCO

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

SCO5550 from the model actinomycete Streptomyces coelicolor A3(2) was identified as a putative transcriptional regulator, and classified into the MerR family by sequence analysis. Recombined SCO5550 was successfully produced in Rhodococcus erythropolis, which can be used to stably express recombinant protein by optimizing the temperature over a wide range (4-35 degrees C). Crystal structure analysis showed that the dimerization domain (C-terminal domain) of SCO5550 has a novel fold and forms a new dimer shape, whereas the DNA-binding domain (N-terminal domain) is very similar to those of MerR family members. Such the new dimer form suggests that SCO5550 may define a new subfamily as a new member of the MerR family. Binding DNA sequence analysis of SCO5550 using the genomic systematic evolution of ligands by exponential enrichment (gSELEX) and electrophoretic mobility shift assay (EMSA) indicated that SCO5550 regulates the expression of the immediately upstream gene sco5551 encoding a putative protein, probably as a transcriptional activator.

Structural and genomic DNA analysis of a putative transcription factor SCO5550 from Streptomyces coelicolor A3(2): regulating the expression of gene sco5551 as a transcriptional activator with a novel dimer shape.,Hayashi T, Tanaka Y, Sakai N, Watanabe N, Tamura T, Tanaka I, Yao M Biochem Biophys Res Commun. 2013 May 24;435(1):28-33. doi:, 10.1016/j.bbrc.2013.04.017. Epub 2013 Apr 22. PMID:23618855[1]

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

References

  1. Hayashi T, Tanaka Y, Sakai N, Watanabe N, Tamura T, Tanaka I, Yao M. Structural and genomic DNA analysis of a putative transcription factor SCO5550 from Streptomyces coelicolor A3(2): regulating the expression of gene sco5551 as a transcriptional activator with a novel dimer shape. Biochem Biophys Res Commun. 2013 May 24;435(1):28-33. doi:, 10.1016/j.bbrc.2013.04.017. Epub 2013 Apr 22. PMID:23618855 doi:http://dx.doi.org/10.1016/j.bbrc.2013.04.017

2dg6, resolution 2.20Å

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