Structural highlights
3ulq is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | |
| Related: | 3q15, 2krf |
| Gene: | rapF, ywhJ, BSU37460 (Bacillus subtilis), comA, comA1, comAA, BSU31680 (Bacillus subtilis) |
| Resources: | FirstGlance, OCA, RCSB, PDBsum |
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]
Publication Abstract from PubMed
The complex interplay between the response regulator ComA, the anti-activator RapF, and the signaling peptide PhrF controls competence development in Bacillus subtilis. More specifically, ComA drives the expression of genetic competence genes, while RapF inhibits the interaction of ComA with its target promoters. The signaling peptide PhrF accumulates at high cell density and upregulates genetic competence by antagonizing the interaction of RapF and ComA. How RapF functions mechanistically to inhibit ComA activity and how PhrF in turn antagonizes the RapF-ComA interaction were unknown. Here we present the X-ray crystal structure of RapF in complex with the ComA DNA binding domain. Along with biochemical and genetic studies, the X-ray crystal structure reveals how RapF mechanistically regulates ComA function. Interestingly, we found that a RapF surface mimics DNA to block ComA binding to its target promoters. Furthermore, RapF is a monomer either alone or in complex with PhrF, and it undergoes a conformational change upon binding to PhrF, which likely causes the dissociation of ComA from the RapF-ComA complex. Finally, we compare the structure of RapF complexed with the ComA DNA binding domain and the structure of RapH complexed with Spo0F. This comparison reveals that RapF and RapH have strikingly similar overall structures, and that they have evolved different, non-overlapping surfaces to interact with diverse cellular targets. To our knowledge, the data presented here reveal the first atomic level insight into the inhibition of response regulator DNA binding by an anti-activator. Compounds that affect the interaction of Rap and Rap-like proteins with their target domains could serve to regulate medically and commercially important phenotypes in numerous Bacillus species, such as sporulation in B. anthracis and sporulation and the production of Cry protein endotoxin in B. thuringiensis.
Structural basis of response regulator inhibition by a bacterial anti-activator protein.,Baker MD, Neiditch MB PLoS Biol. 2011 Dec;9(12):e1001226. Epub 2011 Dec 27. PMID:22215984[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
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
- ↑ Baker MD, Neiditch MB. Structural basis of response regulator inhibition by a bacterial anti-activator protein. PLoS Biol. 2011 Dec;9(12):e1001226. Epub 2011 Dec 27. PMID:22215984 doi:10.1371/journal.pbio.1001226
