Structure of the biofilm matrix promoter AbbA from B. subtilisStructure of the biofilm matrix promoter AbbA from B. subtilis

Structural highlights

2lzf is a 2 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168. 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

YKZF_BACSU

Publication Abstract from PubMed

Bacteria respond to adverse environmental conditions by switching on the expression of large numbers of genes that enable them to adapt to unfavorable circumstances. In Bacillus subtilis, many adaptive genes are under the negative control of the global transition state regulator, the repressor protein AbrB. Stressful conditions lead to the de-repression of genes under AbrB control. Contributing to this de-repression is AbbA, an anti-repressor that binds to and blocks AbrB from binding to DNA. Here, we have determined the NMR structure of the functional AbbA dimer, confirmed that it binds to the N-terminal DNA-binding domain of AbrB, and have provided an initial description for the interaction using computational docking procedures. Interestingly, we show that AbbA has structural and surface characteristics that closely mimic the DNA phosphate backbone, enabling it to readily carry out its physiological function.

A DNA Mimic: The Structure and Mechanism of Action for the Anti-Repressor Protein AbbA.,Tucker AT, Bobay BG, Banse AV, Olson AL, Soderblom EJ, Moseley MA, Thompson RJ, Varney KM, Losick R, Cavanagh J J Mol Biol. 2014 Feb 15. pii: S0022-2836(14)00077-1. doi:, 10.1016/j.jmb.2014.02.010. PMID:24534728[1]

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

References

  1. Tucker AT, Bobay BG, Banse AV, Olson AL, Soderblom EJ, Moseley MA, Thompson RJ, Varney KM, Losick R, Cavanagh J. A DNA Mimic: The Structure and Mechanism of Action for the Anti-Repressor Protein AbbA. J Mol Biol. 2014 Feb 15. pii: S0022-2836(14)00077-1. doi:, 10.1016/j.jmb.2014.02.010. PMID:24534728 doi:http://dx.doi.org/10.1016/j.jmb.2014.02.010
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