9ILL
monomeric SarA-E89Q in complex with DNA
Summary for 9ILL
| Entry DOI | 10.2210/pdb9ill/pdb |
| Descriptor | Transcriptional regulator SarA, DNA (2 entities in total) |
| Functional Keywords | winged-helix protein, complex structure, dna binding protein |
| Biological source | Staphylococcus aureus subsp. aureus N315 More |
| Total number of polymer chains | 3 |
| Total formula weight | 24826.98 |
| Authors | |
| Primary citation | Xia, B.,Fu, D.H. solution Structure of the monomeric SarA in complex with DNA Biomol.NMR Assign, 17:193-197, 2023 Cited by PubMed Abstract: SarA is a global transcription regulator in S. aureus which regulates the expression of over 120 genes related to quorum sensing, biofilm synthesis, drug resistance and many other important physiological processes during host infection. SarA can bind to the promoter region of agr and other target genes to activate or repress the transcription. The crystal structure of SarA uncovered a MarR protein-like conformation with two symmetrical winged helix domains, while its DNA binding mechanism is still unknown. We have constructed a monomeric DNA binding domain of SarA (SarA) for the study of the interaction between SarA and DNA with NMR spectroscopy. Here, we report the H, C and N NMR assignment of SarA/DNA complex which is the first step towards further structure and function analysis. PubMed: 37405582DOI: 10.1007/s12104-023-10140-8 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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