Crystal structure of ribosomal protein L1 from the bacterium <Emphasis Type="Italic">Aquifex aeolicus</Emphasis>

The crystal structure of ribosomal protein L1 from the bacterium Aquifex aeolicus was solved by the molecular-replacement method and refined to R _cryst = 19.4% and R _free = 25.1% at 2.1 Å protein consists of two domains linked together by a flexible hinge region. In the structure under consideration, the domains are in close proximity and adopt a closed conformation. Earlier, this conformation has been found in the structure of protein L1 from the bacterium Thermus thermophilus, whereas the structures of archaeal L1 proteins and the structures of all L1 proteins in the RNA-bound form have an open conformation. The fact that a closed conformation was found in the structures of two L1 proteins which crystallize in different space groups and belong to different bacteria suggests that this conformation is a characteristic feature of L1 bacterial proteins in the free form.     

A generalization of the first Malcev theorem on nilpotent semigroups and nilpotency of the wreath product of semigroups

We describe all [0-]simple semigroups that are nilpotent in the sense of Malcev. This generalizes the first Malcev theorem on nilpotent (in the sense of Malcev) semigroups. It is proved that if the extended standard wreath product of semigroups is nilpotent in the sense of Malcev and the passive semigroup is not nilpotent, then the active semigroup of the wreath product is a finite nilpotent group. In addition to that, the passive semigroup is uniform periodic. Necessary and sufficient conditions are found under which the extended standard wreath product of semigroups is nilpotent in the sense of Malcev in the case where each of the semigroups of the wreath product generates a variety of finite step.