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Ribosomal Protein L1 (ribosomal + protein_l1)
Selected AbstractsHP(2,9)-magainin 2(1,12), a synthetic hybrid peptide, exerts its antifungal effect on Candida albicans by damaging the plasma membraneJOURNAL OF PEPTIDE SCIENCE, Issue 4 2004Yoonkyung Park Abstract In our previous study, HP(2,9)-MA(1,12), HP-MA for short, a hybrid peptide incorporating residues 2,9 of Helicobacter pylori ribosomal protein L1 (HP) and residues 1,12 of magainin 2 (MA) was shown to have strong antibacterial activity. In this study the antifungal activity of HP-MA was evaluated using various fungi, and it was shown that the activity was increased when compared with the parent peptides. In order to investigate the fungicidal mechanism(s) of HP-MA its action against fungal cell membranes was examined by the potassium-release test, which showed that HP-MA caused an increase in the amount of K+ released from the cells. Furthermore, HP-MA induced significant morphological changes. These facts suggested that the fungicidal effect of HP-MA involves damaging the fungal cell membranes. CD investigators suggested that the ,-helical structure of these peptides plays an important role in their antibiotic effect, but that ,-helicity is less directly correlated with the enhanced antibiotic activity of the hybrid. Copyright © 2003 European Peptide Society and John Wiley & Sons, Ltd. [source] Structure of the ribosomal protein L1,mRNA complex at 2.1,Å resolution: common features of crystal packing of L1,RNA complexesACTA CRYSTALLOGRAPHICA SECTION D, Issue 12 2006S. Tishchenko The crystal structure of a hybrid complex between the bacterial ribosomal protein L1 from Thermus thermophilus and a Methanococcus vannielii mRNA fragment containing an L1-binding site was determined at 2.1,Å resolution. It was found that all polar atoms involved in conserved protein,RNA hydrogen bonds have high values of density in the electron-density map and that their hydrogen-bonding capacity is fully realised through interactions with protein atoms, water molecules and K+ ions. Intermolecular contacts were thoroughly analyzed in the present crystals and in crystals of previously determined L1,RNA complexes. It was shown that extension of the RNA helices providing canonical helix stacking between open,open or open,closed ends of RNA fragments is a common feature of these and all known crystals of complexes between ribosomal proteins and RNAs. In addition, the overwhelming majority of complexes between ribosomal proteins and RNA molecules display crystal contacts formed by the central parts of the RNA fragments. These contacts are often very extensive and strong and it is proposed that they are formed in the saturated solution prior to crystal formation. [source] Structure of ribosomal protein L1 from Methanococcus thermolithotrophicus.ACTA CRYSTALLOGRAPHICA SECTION D, Issue 6-2 2002Functionally important structural invariants on the L1 surface The crystal structure of ribosomal protein L1 from the archaeon Methanococcus thermolithotrophicus has been determined at 2.7,Å resolution. The crystals belong to space group P212121, with unit-cell parameters a = 67.0, b = 70.1, c = 106.3,Å and two molecules per asymmetric unit. The structure was solved by the molecular-replacement method with AMoRe and refined with CNS to an R value of 18.9% and an Rfree of 25.4% in the resolution range 30,2.7,Å. Comparison of this structure with those obtained previously for two L1 proteins from other sources (the bacterium Thermus thermophilus and the archaeon M. jannaschii) as well as detailed analysis of intermolecular contacts in the corresponding L1 crystals reveal structural invariants on the molecular surface which are probably important for binding the 23S ribosomal RNA and protein function within the ribosome. [source] | ||||||||||