7a9a

Crystal structure of rubredoxin B (Rv3250c) from Mycobacterium tuberculosis

spinqualitylabelsall models 7a9a, resolution 1.17Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7a9a is a 8 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.17Å Ligands: CL, EDO, FE, GOL, PEG, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function I6YFL7_MYCTU Involved in the hydrocarbon hydroxylating system, which transfers electrons from NADH to rubredoxin reductase and then through rubredoxin to alkane 1 monooxygenase.[ARBA:ARBA00002792] Publication Abstract from PubMed Electron transfer mediated by metalloproteins drives many biological processes. Rubredoxins are a ubiquitous [1Fe-0S] class of electron carriers that play an important role in bacterial adaptation to changing environmental conditions. In Mycobacterium tuberculosis, oxidative and acidic stresses as well as iron starvation induce rubredoxins expression. However, their functions during M. tuberculosis infection are unknown. In the present work, we show that rubredoxin B (RubB) is able to efficiently shuttle electrons from cognate reductases, FprA and FdR to support catalytic activity of cytochrome P450s, CYP124, CYP125, and CYP142, which are important for bacterial viability and pathogenicity. We solved the crystal structure of RubB and characterized the interaction between RubB and CYPs using site-directed mutagenesis. Mutations that not only neutralize single charge but also change the specific residues on the surface of RubB did not dramatically decrease activity of studied CYPs. Together with isothermal calorimetry (ITC) experiments, the obtained results suggest that interactions are transient and not highly specific. The redox potential of RubB is -264 mV vs. Ag/AgCl and the measured extinction coefficients are 9931 M(-1)cm(-1) and 8371 M(-1)cm(-1) at 380 nm and 490 nm, respectively. Characteristic parameters of RubB along with the discovered function might be useful for biotechnological applications. Our findings suggest that a switch from ferredoxins to rubredoxins might be crucial for M. tuberculosis to support CYPs activity during the infection. A new twist of rubredoxin function in M. tuberculosis.,Sushko T, Kavaleuski A, Grabovec I, Kavaleuskaya A, Vakhrameev D, Bukhdruker S, Marin E, Kuzikov A, Masamrekh R, Shumyantseva V, Tsumoto K, Borshchevskiy V, Gilep A, Strushkevich N Bioorg Chem. 2021 Feb 11;109:104721. doi: 10.1016/j.bioorg.2021.104721. PMID:33618255 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Rubredoxin 3D structures

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