7bme
From Proteopedia
Jump to navigationJump to search
Crystal structure of a R18W mutant of the DNA-binding protein RemA from Geobacillus thermodenitrificans
| ||||||||||||
Structural highlights
FunctionPublication Abstract from PubMedBacillus subtilis can form structurally complex biofilms on solid or liquid surfaces, which requires expression of genes for matrix production. The transcription of these genes is activated by regulatory protein RemA, which binds to poorly conserved, repetitive DNA regions but lacks obvious DNA-binding motifs or domains. Here, we present the structure of the RemA homologue from Geobacillus thermodenitrificans, showing a unique octameric ring with the potential to form a 16-meric superstructure. These results, together with further biochemical and in vivo characterization of B. subtilis RemA, suggests that the protein can wrap DNA around its ring-like structure through a LytTR-related domain. Structural and functional characterization of the bacterial biofilm activator RemA.,Hoffmann T, Mrusek D, Bedrunka P, Burchert F, Mais CN, Kearns DB, Altegoer F, Bremer E, Bange G Nat Commun. 2021 Sep 29;12(1):5707. doi: 10.1038/s41467-021-26005-4. PMID:34588455[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||
This page was last modified 12:30, 1 February 2024.