6KO7
Crystal structure of the Ethidium bound RamR determined with XtaLAB Synergy
Summary for 6KO7
Entry DOI | 10.2210/pdb6ko7/pdb |
Descriptor | Putative regulatory protein, ETHIDIUM, SULFATE ION, ... (4 entities in total) |
Functional Keywords | multisite binding pocket, hth-motif, dna binding protein |
Biological source | Salmonella enterica subsp. enterica serovar Typhimurium str. 14028S |
Total number of polymer chains | 4 |
Total formula weight | 89818.92 |
Authors | Matsumoto, T.,Nakashima, R.,Yamano, A.,Nishino, K. (deposition date: 2019-08-08, release date: 2019-10-09, Last modification date: 2023-11-22) |
Primary citation | Matsumoto, T.,Nakashima, R.,Yamano, A.,Nishino, K. Development of a structure determination method using a multidrug-resistance regulator protein as a framework. Biochem.Biophys.Res.Commun., 518:402-408, 2019 Cited by PubMed Abstract: The structure determination of organic compounds is desirable for the development of medicines, aroma chemicals, and agricultural chemicals. However, the crystallization of organic compounds is often troublesome, because crystallization requires a relatively large quantity of high purity compounds and crystallization trials often need to be performed repetitively using different conditions. Some proteins are known to be able to bind to various organic compounds. The multidrug-resistance regulator protein RamR is one such protein. We have developed a structure determination method for organic compounds using RamR. RamR bound to organic compounds, including one compound that was not a known ligand for RamR, and the structures of the complexes were successfully determined. Because the RamR crystal is hydrophilic, this method may be useful for compounds that cannot be handled by the crystalline sponge method. PubMed: 31431261DOI: 10.1016/j.bbrc.2019.08.070 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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