3S8Q

Crystal structure of the R-M controller protein C.Esp1396I OL operator complex

Summary for 3S8Q

• Entry DOI: 10.2210/pdb3s8q/pdb
• Related: 3CLC 3FYA 3G5G
• Descriptor: R-M CONTROLLER PROTEIN, DNA (5'-D(*AP*TP*GP*TP*GP*AP*CP*TP*TP*AP*TP*AP*GP*TP*CP*CP*GP*TP*G)-3'), DNA (5'-D(*TP*CP*AP*CP*GP*GP*AP*CP*TP*AP*TP*AP*AP*GP*TP*CP*AP*CP*A)-3'), ... (4 entities in total)
• Functional Keywords: protein-dna complex, helix-turn-helix, transcriptional regulator, dna-binding protein, protein binding-dna complex, protein binding/dna
• Biological source: Enterobacter sp. RFL1396
• Total number of polymer chains: 4
• Total formula weight: 30690.93

Authors

McGeehan, J.E.,Ball, N.J.,Streeter, S.D.,Thresh, S.-J.,Kneale, G.G. (deposition date: 2011-05-30, release date: 2012-01-18, Last modification date: 2024-02-28)

Primary citation

McGeehan, J.E.,Ball, N.J.,Streeter, S.D.,Thresh, S.J.,Kneale, G.G.
Recognition of dual symmetry by the controller protein C.Esp1396I based on the structure of the transcriptional activation complex.
Nucleic Acids Res., 40:4158-4167, 2012

PubMed Abstract: The controller protein C.Esp1396I regulates the timing of gene expression of the restriction-modification (RM) genes of the RM system Esp1396I. The molecular recognition of promoter sequences by such transcriptional regulators is poorly understood, in part because the DNA sequence motifs do not conform to a well-defined symmetry. We report here the crystal structure of the controller protein bound to a DNA operator site. The structure reveals how two different symmetries within the operator are simultaneously recognized by the homo-dimeric protein, underpinned by a conformational change in one of the protein subunits. The recognition of two different DNA symmetries through movement of a flexible loop in one of the protein subunits may represent a general mechanism for the recognition of pseudo-symmetric DNA sequences.

PubMed: 22210861
DOI: 10.1093/nar/gkr1250

Experimental method

X-RAY DIFFRACTION (2.1 Å)