1umq: Difference between revisions
m Protected "1umq" [edit=sysop:move=sysop] |
No edit summary |
||
| (10 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
< | ==solution structure and DNA binding of the effector domain from the global regulator PrrA(RegA) from R. sphaeroides: Insights into DNA binding specificity== | ||
<StructureSection load='1umq' size='340' side='right'caption='[[1umq]]' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1umq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UMQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UMQ FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1umq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1umq OCA], [https://pdbe.org/1umq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1umq RCSB], [https://www.ebi.ac.uk/pdbsum/1umq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1umq ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/REGA_CERS4 REGA_CERS4] Member of the two-component regulatory system RegB/RegA. Involved in transactivating anaerobic expression of the photosynthetic apparatus. It is a transcriptional regulator that is responsible for activating expression of the puf, puh, and puc operons in response to a decrease in oxygen tension. | |||
== 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/um/1umq_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1umq ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Prr/RegA response regulator is a global transcription regulator in purple bacteria Rhodobacter sphaeroides and Rhodobacter capsulatus, and is essential in controlling the metabolic changes between aerobic and anaerobic environments. We report here the structure determination by NMR of the C-terminal effector domain of PrrA, PrrAC. It forms a three-helix bundle containing a helix-turn-helix DNA binding motif. The fold is similar to FIS protein, but the domain architecture is different from previously characterised response regulator effector domains, as it is shorter than any characterised so far. Alignment of Prr/RegA DNA targets permitted a refinement of the consensus sequence, which contains two GCGNC inverted repeats with variable half-site spacings. NMR titrations of PrrAC with specific and non-specific DNA show which surfaces are involved in DNA binding and suggest residues important for binding specificity. A model of the PrrAC/DNA complex was constructed in which two PrrAC molecules are bound to DNA in a symmetrical manner. | |||
Solution structure and DNA binding of the effector domain from the global regulator PrrA (RegA) from Rhodobacter sphaeroides: insights into DNA binding specificity.,Laguri C, Phillips-Jones MK, Williamson MP Nucleic Acids Res. 2003 Dec 1;31(23):6778-87. PMID:14627811<ref>PMID:14627811</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1umq" style="background-color:#fffaf0;"></div> | |||
== | |||
==See Also== | ==See Also== | ||
*[[Response regulator 3D structure|Response regulator 3D structure]] | |||
*[[Response regulator|Response regulator]] | == References == | ||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: | [[Category: Cereibacter sphaeroides]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Laguri C]] | ||
[[Category: | [[Category: Phillips-Jones MK]] | ||
[[Category: Williamson MP]] | |||
[[Category: | |||
Latest revision as of 08:59, 19 June 2024
solution structure and DNA binding of the effector domain from the global regulator PrrA(RegA) from R. sphaeroides: Insights into DNA binding specificitysolution structure and DNA binding of the effector domain from the global regulator PrrA(RegA) from R. sphaeroides: Insights into DNA binding specificity
Structural highlights
FunctionREGA_CERS4 Member of the two-component regulatory system RegB/RegA. Involved in transactivating anaerobic expression of the photosynthetic apparatus. It is a transcriptional regulator that is responsible for activating expression of the puf, puh, and puc operons in response to a decrease in oxygen tension. 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 PubMedPrr/RegA response regulator is a global transcription regulator in purple bacteria Rhodobacter sphaeroides and Rhodobacter capsulatus, and is essential in controlling the metabolic changes between aerobic and anaerobic environments. We report here the structure determination by NMR of the C-terminal effector domain of PrrA, PrrAC. It forms a three-helix bundle containing a helix-turn-helix DNA binding motif. The fold is similar to FIS protein, but the domain architecture is different from previously characterised response regulator effector domains, as it is shorter than any characterised so far. Alignment of Prr/RegA DNA targets permitted a refinement of the consensus sequence, which contains two GCGNC inverted repeats with variable half-site spacings. NMR titrations of PrrAC with specific and non-specific DNA show which surfaces are involved in DNA binding and suggest residues important for binding specificity. A model of the PrrAC/DNA complex was constructed in which two PrrAC molecules are bound to DNA in a symmetrical manner. Solution structure and DNA binding of the effector domain from the global regulator PrrA (RegA) from Rhodobacter sphaeroides: insights into DNA binding specificity.,Laguri C, Phillips-Jones MK, Williamson MP Nucleic Acids Res. 2003 Dec 1;31(23):6778-87. PMID:14627811[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
| ||||||||||||||||