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7P1W

Crystal structure of a R51 R53 double mutant of the DNA-binding protein RemA from Geobacillus thermodenitrificans

Summary for 7P1W
Entry DOI10.2210/pdb7p1w/pdb
Related7BM2
DescriptorPutative regulatory protein GTNG_1019 (2 entities in total)
Functional Keywordsbiofilm, dna-binding, histone-like, geobacillus, dna binding protein
Biological sourceGeobacillus thermodenitrificans (strain NG80-2)
Total number of polymer chains2
Total formula weight20605.32
Authors
Altegoer, F.,Mrusek, D.,Bange, G. (deposition date: 2021-07-02, release date: 2021-08-25, Last modification date: 2024-01-31)
Primary citationHoffmann, T.,Mrusek, D.,Bedrunka, P.,Burchert, F.,Mais, C.N.,Kearns, D.B.,Altegoer, F.,Bremer, E.,Bange, G.
Structural and functional characterization of the bacterial biofilm activator RemA.
Nat Commun, 12:5707-5707, 2021
Cited by
PubMed Abstract: Bacillus 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.
PubMed: 34588455
DOI: 10.1038/s41467-021-26005-4
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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