9ill

From Proteopedia

monomeric SarA-E89Q in complex with DNA

Structural highlights

9ill is a 3 chain structure with sequence from Staphylococcus aureus subsp. aureus N315 and Synthetic construct. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 20 models
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SARA_STAAN Global regulator with both positive and negative effects that controls the expression of several virulence factors and the biofilm formation process in a cell density-dependent manner.

Publication Abstract from PubMed

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(DeltaN19)) for the study of the interaction between SarA and DNA with NMR spectroscopy. Here, we report the (1)H, (13)C and (15)N NMR assignment of SarA(DeltaN19)/DNA complex which is the first step towards further structure and function analysis.

(1)H, (13)C, and (15)N resonance assignments of SarA monomer from Staphylococcus aureus in complex with DNA.,Fu D, Duan B, Dong X, Xia B Biomol NMR Assign. 2023 Dec;17(2):193-197. doi: 10.1007/s12104-023-10140-8. Epub , 2023 Jul 5. PMID:37405582^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Fu D, Duan B, Dong X, Xia B. (1)H, (13)C, and (15)N resonance assignments of SarA monomer from Staphylococcus aureus in complex with DNA. Biomol NMR Assign. 2023 Dec;17(2):193-197. PMID:37405582 doi:10.1007/s12104-023-10140-8