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2krf

From Proteopedia

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Current revision

NMR 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.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CMPA_BACSU Response regulator in the two-component regulatory system ComP/ComA involved in a major quorum response pathway that regulates the development of genetic competence. Regulates directly the expression of over 20 genes, including genes of the srfA operon, degQ, rapA, rapC, rapE, rapF, etc. Regulates indirectly, through the regulation of comK transcription, the expression of late competence genes.^[1]

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^[2]

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

References

↑ Comella N, Grossman AD. Conservation of genes and processes controlled by the quorum response in bacteria: characterization of genes controlled by the quorum-sensing transcription factor ComA in Bacillus subtilis. Mol Microbiol. 2005 Aug;57(4):1159-74. PMID:16091051 doi:http://dx.doi.org/MMI4749
↑ 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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2krf"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2krf]] 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=2KRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KRF FirstGlance]. <br>
-</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=2krf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2krf OCA], [https://pdbe.org/2krf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2krf RCSB], [https://www.ebi.ac.uk/pdbsum/2krf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2krf ProSAT]</span></td></tr>
+</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=2krf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2krf OCA], [https://pdbe.org/2krf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2krf RCSB], [https://www.ebi.ac.uk/pdbsum/2krf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2krf ProSAT]</span></td></tr>
 </table>
 == Function ==

2krf

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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