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6KO7

Crystal structure of the Ethidium bound RamR determined with XtaLAB Synergy

Summary for 6KO7
Entry DOI10.2210/pdb6ko7/pdb
DescriptorPutative regulatory protein, ETHIDIUM, SULFATE ION, ... (4 entities in total)
Functional Keywordsmultisite binding pocket, hth-motif, dna binding protein
Biological sourceSalmonella enterica subsp. enterica serovar Typhimurium str. 14028S
Total number of polymer chains4
Total formula weight89818.92
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 citationMatsumoto, 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: 31431261
DOI: 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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