Sandbox Reserved 1501

This Sandbox is Reserved from 06/12/2018, through 30/06/2019 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1480 through Sandbox Reserved 1543.

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spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Relevance While the function of cytochrome b2 is to couple L-lactate dehydrogenation to cytochrome c reduction; the mutant ARG289LYS is changing the kinetics of the reactions. It is rising the Ki of several components in comparison to the wild-type, while kcat and KM are also changed by a factor of 10. It changes also the induction by L-lactate. R289K-b(2) eing a component of the mitochondrial inter membrane space Structural highlights Global Symmetry Cyclic - C4 Global Stoichiometry Homotetramer A4 Flavocytochrome b(2) is a tetrameric enzyme [Jacq and Lederer, 1972]. Each of the four identical subunits is composed by one single polypeptide chain. Each subunit contains a binding site for the selectively non-covalently binding of the cofactor FM3- (FlavinMonoNucleotide), heme b(2) cofactor [[right |center|border|180x180px|Image:Flav.png]] Image:Flav.png  [[Flavinmononucleotide |center|border|180x180px|Image:Hfdbtg.JPG]] Image:Hfdbtg.JPG  [[heme b(2) cofactor |center|border|180x180px|]]   https://www.wikiwand.com/de/Flavinmononukleotid as well as one in with the iron complexed in the tetrapyrrole ring interacts with heme b(2-) cofactor [Risler and Groudinsky, 1973]. https://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60344 The amino acid sequence in the heme binding region was first determined by Guidard et al. (1974). For every subunit the crystallized preparation analysis determined a molecular weight of the chain of 36 kD [Appleby and Morton] and the chain of 21 kD [Jacq and Lederer, 1974]. Arginin 289 to Lysine https://www.worthington-biochem.com/yldhs/

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