Results of U-Pb dating of zircon and baddeleyite from the Noril'sk-1 ultramafic-mafic intrusion (Russia)

We present for the first time the mineralogical and isotope-geochemical particularities of zircon and baddeleyite from various rocks of the economic ore-bearing Noril'sk-1 intrusion located in the northwestern part of the Siberian platform. The ultramafic-mafic Noril'sk-1 intrusion hosts one of the world's major economic platinum-group-element (PGE)-Cu-Ni sulphide deposits. A detailed study of crystal morphology and internal structure identify four zircon populations, characterized by different U-Pb (SHRIMP-II) ages. The U-Pb ages of baddeleyite and the defined zircon populations cover a significant time span (from 290 ± 2.8 to 226.7 ± 0.9 Ma). The established U-Pb ages imply that crystallization of baddeleyite and zircon populations corresponds to several stages of protracted evolution of the ore-forming magmatic system (290 ± 2.8, 261.3 ± 1.6, 245.7 ± 1.1, 236.5 ± 1.8, and 226.7 ± 0.9 Ma, respectively) that served as the favorable factor for accumulatio n of magmas and ores of unique scales and concentrations.8 page(s

Crystal structure of pyruvate dehydrogenase kinase 3 bound to lipoyl domain 2 of human pyruvate dehydrogenase complex

The human pyruvate dehydrogenase complex (PDC) is regulated by reversible phosphorylation by four isoforms of pyruvate dehydrogenase kinase (PDK). PDKs phosphorylate serine residues in the dehydrogenase (E1p) component of PDC, but their amino-acid sequences are unrelated to eukaryotic Ser/Thr/Tyr protein kinases. PDK3 binds to the inner lipoyl domains (L2) from the 60-meric transacetylase (E2p) core of PDC, with concomitant stimulated kinase activity. Here, we present crystal structures of the PDK3–L2 complex with and without bound ADP or ATP. These structures disclose that the C-terminal tail from one subunit of PDK3 dimer constitutes an integral part of the lipoyl-binding pocket in the N-terminal domain of the opposing subunit. The two swapped C-terminal tails promote conformational changes in active-site clefts of both PDK3 subunits, resulting in largely disordered ATP lids in the ADP-bound form. Our structural and biochemical data suggest that L2 binding stimulates PDK3 activity by disrupting the ATP lid, which otherwise traps ADP, to remove product inhibition exerted by this nucleotide. We hypothesize that this allosteric mechanism accounts, in part, for E2p-augmented PDK3 activity