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Crystal structure of Bacillus subtilis YmdB, a global regulator of late adaptive responses.Crystal structure of Bacillus subtilis YmdB, a global regulator of late adaptive responses.
Structural highlights
FunctionPublication Abstract from PubMedBacillus subtilis mutants lacking ymdB are unable to form biofilms, exhibit a strong overexpression of the flagellin gene hag, and are deficient in SlrR, a SinR antagonist. Here, we report the functional and structural characterization of YmdB, and we find that YmdB is a phosphodiesterase with activity against 2',3'- and 3',5'-cyclic nucleotide monophosphates. The structure of YmdB reveals that the enzyme adopts a conserved phosphodiesterase fold with a binuclear metal center. Mutagenesis of a catalytically crucial residue demonstrates that the enzymatic activity of YmdB is essential for biofilm formation. The deletion of ymdB affects the expression of more than 800 genes; the levels of the sigma(D)-dependent motility regulon and several sporulation genes are increased, and the levels of the SinR-repressed biofilm genes are decreased, confirming the role of YmdB in regulating late adaptive responses of B. subtilis. The YmdB Phosphodiesterase Is a Global Regulator of Late Adaptive Responses in Bacillus subtilis.,Diethmaier C, Newman JA, Kovacs AT, Kaever V, Herzberg C, Rodrigues C, Boonstra M, Kuipers OP, Lewis RJ, Stulke J J Bacteriol. 2014 Jan;196(2):265-75. doi: 10.1128/JB.00826-13. Epub 2013 Oct 25. PMID:24163345[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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