Structure of cytochrome b 5 unique to tardigrades
نویسندگان
چکیده
منابع مشابه
The binding of cytochrome b 5 to liver microsomes.
The 40-44 hydrophobic peptide segment, present in cytochrome bS obtained by nonhydrolytic means, but absent from lipase or trypsin-extracted cytochrome bg, has been found to be required for the binding of a loto 20-fold molar excess of cytochrome bs to liver microsomes. At saturation, the bound cytochrome bs constitutes nearly 20% of the total protein of the vesicle preparations. This extra bou...
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Using 1617 meaningful NOEs with 188 pseudocontact shifts, a family of 35 conformers of oxidized bovine microsomal cytochrome b5 mutant (E44/48/56A/D60A) has been obtained and is characterized by good resolution (rmsd to the mean structure are 0.047 +/- 0.007 nm and 0.095 +/- 0.008 nm for backbone and heavy atoms, respectively). The solution structure of the mutant, when compared with the X-ray ...
متن کاملTardigrades
Tardi-what? Tardigrades, also known as water bears, are a littlestudied phylum of animals. First discovered 230 years ago, there are at least 700 different species living on land, in fresh water and in the sea. The tardigrades represent a successful group of animals — in flourishing existence after about 600 million years of evolution — that could hold keys to the patterns and mechanisms by whi...
متن کاملThe reactivity of the tyrosyl residues of cytochrome b 5 .
The reactivities of the tyrosyl residues of calf and rabbit cytochrome bs have been examined by acylation, iodination, and titration of the proteins. These experiments distinguish residues 6 and 7 as the most exposed and reactive residues, which ionize normally and can be acetylated or iodinated to form the monoiodo or diiodo derivatives. Tyrosine 30, which is common to both cytochrome preparat...
متن کاملEnhancement of cytochrome P-450 3A4 catalytic activities by cytochrome b(5) in bacterial membranes.
Activities of testosterone, nifedipine, and midazolam oxidation by recombinant cytochrome P-450 (P-450) 3A4 coexpressed with human NADPH-P-450 reductase (NPR) in bacterial membranes (CYP3A4/NPR membranes) were determined in comparison with those of other recombinant systems and of human liver microsomes with high contents of CYP3A4. Growth conditions for Escherichia coli transformed with the bi...
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ژورنال
عنوان ژورنال: Protein Science
سال: 2020
ISSN: 0961-8368,1469-896X
DOI: 10.1002/pro.3896