2krf: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
m Protected "2krf" [edit=sysop:move=sysop]
No edit summary
Line 1: Line 1:
[[Image:2krf.png|left|200px]]
==NMR solution structure of the DNA binding domain of Competence protein A==
<StructureSection load='2krf' size='340' side='right' caption='[[2krf]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2krf]] 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=2KRF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KRF FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BSU31680, comA, comA1, comAA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</td></tr>
<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=2krf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2krf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2krf RCSB], [http://www.ebi.ac.uk/pdbsum/2krf PDBsum]</span></td></tr>
</table>
== 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/kr/2krf_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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Competence protein A (ComA) is a response regulator protein involved in the development of genetic competence in the Gram-positive spore-forming bacterium Bacillus subtilis, as well as the regulation of the production of degradative enzymes and antibiotic synthesis. ComA belongs to the NarL family of proteins, which are characterized by a C-terminal transcriptional activator domain that consists of a bundle of four helices, where the second and third helices (alpha 8 and alpha 9) form a helix-turn-helix DNA-binding domain. Using NMR spectroscopy, the high-resolution 3D solution structure of the C-terminal DNA-binding domain of ComA (ComAC) has been determined. In addition, surface plasmon resonance and NMR protein-DNA titration experiments allowed for the analysis of the interaction of ComAC with its target DNA sequences. Combining the solution structure and biochemical data, a model of ComAC bound to the ComA recognition sequences on the srfA promoter has been developed. The model shows that for DNA binding, ComA uses the conserved helix-turn-helix motif present in other NarL family members. However, the model reveals also that ComA might use a slightly different part of the helix-turn-helix motif and there appears to be some associated domain re-orientation. These observations suggest a basis for DNA binding specificity within the NarL family.


{{STRUCTURE_2krf|  PDB=2krf  |  SCENE=  }}
NMR solution structure and DNA-binding model of the DNA-binding domain of competence protein A.,Hobbs CA, Bobay BG, Thompson RJ, Perego M, Cavanagh J J Mol Biol. 2010 Apr 30;398(2):248-63. Epub 2010 Mar 17. PMID:20302877<ref>PMID:20302877</ref>


===NMR solution structure of the DNA binding domain of Competence protein A===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_20302877}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[2krf]] 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=2KRF OCA].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:020302877</ref><references group="xtra"/>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Bobay, B G.]]
[[Category: Bobay, B G.]]

Revision as of 18:37, 12 October 2014

NMR solution structure of the DNA binding domain of Competence protein ANMR solution structure of the DNA binding domain of Competence protein A

Structural highlights

2krf is a 2 chain structure with sequence from Bacillus subtilis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:BSU31680, comA, comA1, comAA (Bacillus subtilis)
Resources:FirstGlance, OCA, RCSB, PDBsum

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

Competence protein A (ComA) is a response regulator protein involved in the development of genetic competence in the Gram-positive spore-forming bacterium Bacillus subtilis, as well as the regulation of the production of degradative enzymes and antibiotic synthesis. ComA belongs to the NarL family of proteins, which are characterized by a C-terminal transcriptional activator domain that consists of a bundle of four helices, where the second and third helices (alpha 8 and alpha 9) form a helix-turn-helix DNA-binding domain. Using NMR spectroscopy, the high-resolution 3D solution structure of the C-terminal DNA-binding domain of ComA (ComAC) has been determined. In addition, surface plasmon resonance and NMR protein-DNA titration experiments allowed for the analysis of the interaction of ComAC with its target DNA sequences. Combining the solution structure and biochemical data, a model of ComAC bound to the ComA recognition sequences on the srfA promoter has been developed. The model shows that for DNA binding, ComA uses the conserved helix-turn-helix motif present in other NarL family members. However, the model reveals also that ComA might use a slightly different part of the helix-turn-helix motif and there appears to be some associated domain re-orientation. These observations suggest a basis for DNA binding specificity within the NarL family.

NMR solution structure and DNA-binding model of the DNA-binding domain of competence protein A.,Hobbs CA, Bobay BG, Thompson RJ, Perego M, Cavanagh J J Mol Biol. 2010 Apr 30;398(2):248-63. Epub 2010 Mar 17. PMID:20302877[1]

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

References

  1. Hobbs CA, Bobay BG, Thompson RJ, Perego M, Cavanagh J. NMR solution structure and DNA-binding model of the DNA-binding domain of competence protein A. J Mol Biol. 2010 Apr 30;398(2):248-63. Epub 2010 Mar 17. PMID:20302877 doi:10.1016/j.jmb.2010.03.003
Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA