Genetic variants are associated with childhood neurodegeneration and Alzheimer's disease; however, the molecular function of ceroid lipofuscinosis neuronal protein 5 (Cln5) is unknown. We solved the Cln5 crystal structure and identified a region homologous to the catalytic domain of members of the N1pC/P60 superfamily of papain-like enzymes. However, we observed no protease activity for Cln5; and instead, we discovered that Cln5 and structurally related PPPDE1 and PPPDE2 have efficient cysteine palmitoyl thioesterase (-depalmitoylation) activity using fluorescent substrates.
View Article and Find Full Text PDFThe cyclic alkyl(amino) carbene (cAAC) anchored silylene with two phosphinidenes was isolated as (cAAC)Si{P(cAAC)} (3) at room temperature, which was synthesized from the reduction of (Cl)Si{P(cAAC)} (2) using 2 equiv of KC. Compound 2 resulted from the reaction of 2 equiv of (cAAC)PK (1) with 1 equiv of SiCl. Compounds 2 and 3 are the first examples where two terminal phosphinidenes are binding each to a silicon center characterized by single crystal X-ray structural analysis.
View Article and Find Full Text PDFThe cyclic alkyl(amino) carbene (cAAC) stabilized monoanionic phosphorus atom in the form of lithium phosphinidene [cAACPLi(THF)] (1) has been isolated as a molecular species and characterized by single crystal X-ray structure analysis. Furthermore, the structure and bonding of compound 1 has been investigated by theoretical methods. The utilization of the lithium phosphinidene as a phosphorus transfer reagent for a wide range of organic and inorganic substrates has been investigated.
View Article and Find Full Text PDFThe cyclic alkyl(amino) carbene (cAAC) stabilized biradicals of composition (cAAC)SiH (1), (cAAC)SiMe-SiMe(cAAC) (2), and (cAAC)SiMeCl-SiMeCl(cAAC) (3) have been isolated as molecular species. All the compounds are stable at room temperature for more than 6 months under inert conditions in the solid state. All radical species were fully characterized by single-crystal X-ray structure analysis and EPR spectroscopy.
View Article and Find Full Text PDFJ Appl Crystallogr
February 2014
Some of the improvements in make convenient to use for refinement of macromolecular structures against neutron data without the support of X-ray data. The new NEUT instruction adjusts the behaviour of the SFAC instruction as well as the default bond lengths of the AFIX instructions. This work presents a protocol on how to use for refinement of protein structures against neutron data.
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