2ro4

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==RDC-refined Solution Structure of the N-terminal DNA Recognition Domain of the Bacillus subtilis Transition-state Regulator AbrB==
==RDC-refined Solution Structure of the N-terminal DNA Recognition Domain of the Bacillus subtilis Transition-state Regulator AbrB==
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<StructureSection load='2ro4' size='340' side='right' caption='[[2ro4]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
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<StructureSection load='2ro4' size='340' side='right'caption='[[2ro4]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2ro4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RO4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RO4 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2ro4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RO4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RO4 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1z0r|1z0r]], [[2fy9|2fy9]], [[2ro3|2ro3]], [[2ro5|2ro5]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">abrB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ro4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ro4 OCA], [https://pdbe.org/2ro4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ro4 RCSB], [https://www.ebi.ac.uk/pdbsum/2ro4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ro4 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ro4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ro4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ro4 RCSB], [http://www.ebi.ac.uk/pdbsum/2ro4 PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ABRB_BACSU ABRB_BACSU]] Ambiactive repressor and activator of the transcription of genes expressed during the transition state between vegetative growth and the onset of stationary phase and sporulation. It controls the expression of genes spovG and tycA. AbrB binds to the tycA promoter region at two A- and T-rich sites, it may be the sole repressor of tycA transcription.<ref>PMID:2504584</ref>
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[https://www.uniprot.org/uniprot/ABRB_BACSU ABRB_BACSU] Ambiactive repressor and activator of the transcription of genes expressed during the transition state between vegetative growth and the onset of stationary phase and sporulation. It controls the expression of genes spovG and tycA. AbrB binds to the tycA promoter region at two A- and T-rich sites, it may be the sole repressor of tycA transcription.<ref>PMID:2504584</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ro/2ro4_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ro/2ro4_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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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/chain_selection.php?pdb_ID=2ata ConSurf].
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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=2ro4 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Understanding the DNA recognition and binding by the AbrB-like family of transcriptional regulators is of significant interest since these proteins enable bacteria to elicit the appropriate response to diverse environmental stimuli. Although these "transition-state regulator" proteins have been well characterized at the genetic level, the general and specific mechanisms of DNA binding remain elusive. We present RDC-refined NMR solution structures and dynamic properties of the DNA-binding domains of three Bacillus subtilis transition-state regulators: AbrB, Abh, and SpoVT. We combined previously investigated DNase I footprinting, DNA methylation, gel-shift assays, and mutagenic and NMR studies to generate a structural model of the complex between AbrBN(55) and its cognate promoter, abrB8. These investigations have enabled us to generate a model for the specific nature of the transition-state regulator-DNA interaction, a structure that has remained elusive thus far.
 
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Insights into the nature of DNA binding of AbrB-like transcription factors.,Sullivan DM, Bobay BG, Kojetin DJ, Thompson RJ, Rance M, Strauch MA, Cavanagh J Structure. 2008 Nov 12;16(11):1702-13. PMID:19000822<ref>PMID:19000822</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Bobay, B G]]
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[[Category: Large Structures]]
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[[Category: Cavanagh, J]]
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[[Category: Bobay BG]]
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[[Category: Kojetin, D J]]
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[[Category: Cavanagh J]]
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[[Category: Rance, M]]
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[[Category: Kojetin DJ]]
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[[Category: Strauch, M A]]
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[[Category: Rance M]]
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[[Category: Sullivan, D M]]
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[[Category: Strauch MA]]
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[[Category: Thompson, R J]]
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[[Category: Sullivan DM]]
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[[Category: Activator]]
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[[Category: Thompson RJ]]
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[[Category: Dna-binding]]
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[[Category: Repressor]]
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[[Category: Sporulation]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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Current revision

RDC-refined Solution Structure of the N-terminal DNA Recognition Domain of the Bacillus subtilis Transition-state Regulator AbrB

PDB ID 2ro4

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