Three-dimensional structures bacteriophage

Thiosulfate cyanide sulfurtransferase symmetry in 78 TTiiouridine 234 Three-dimensional structures of aconitase 689 adenylate kinase 655 aldehyde oxido-reductase 891 D-amino acid oxidase 791 a-amylase, pancreatic 607 aspartate aminotransferase 57,135 catalytic intermediates 752 aspartate carbamyltransferase 348 aspartate chemoreceptor 562 bacteriophage P22 66 cadherin 408 calmodulin 317 carbonic acid anhydrase I 679 carboxypeptidase A 64 catalase 853 cholera toxin 333, 546 chymotrypsin 611 citrate synthase 702, 703 cutinase 134 cyclosporin 488 cytochrome c 847 cytochrome c peroxidase 849 dihydrofolate reductase 807 DNA 214, 223,228,229, 241 DNA complex... 

FIGURE 1. Three-dimensional structure of catalytic core regions in Escherichia coli class I (A) and bacteriophage T4 class III (B) RNRs (Logan et ai, 1999 Uhlin and Eklund, 1994). The ten-stranded p/a barrel comprising the active site region is shown. The finger-loop, which contains the active site cysteine, is shown as a solid line. 

The three-dimensional structure of the class III RNR from bacteriophage T4 was recently solved to high resolution for the mutant enzyme G580A, which has an alanine residue at the position of the stable glycyl radical in the native enzyme (Logan et al., 1999). This prevents oxygen-dependent irreversible truncation of the polypeptide chain (Young et al., 1996). The three-dimensional structure of the mutant enzyme showed that... 

Lysozymes derived from sources other than bird egg-whites were also tested for their susceptibility to inactivation by the epoxypropyl /8-gly-cosides. Among these, human leukemic urine lysozyme was inactivated by (GlcNAc)3-Ep at pH 5.5, whereas the lysozymes from papaya latex and the bacteriophage T4 were not inactivated at all. Similar results were also obtained at pH 4.6, at which the papaya lysozyme acts on chitin most efficiently. These results show that the active sites of human and the hen lysozymes are similar, whereas the active sites of the T4 phage and the papaya lysozymes differ from them. Indeed, the hen and the human lysozymes are similar in their amino acid sequences" and three-dimensional structures, whereas the papaya and the T4 phage lysozymes differ from the hen egg-w hite lysozyme in their amino acid composition, molecular weight, and substrate specificity."" ... 

The three-dimensional structure of lysozyme from bacteriophage T4 has been determined at 2.5 A resolution. The structure differs from that of hen egg-white lysozyme, although it is not clear whether or not the mechanisms of catalysis of the enzymes are related. Other physical properties, including the reversible unfolding, of bacteriophage T4 lysozyme have been reported. ... 

Both X-ray and neutron fiber diffraction (as well as electron microscopy) techniques have been applied to filamentous viruses, for which the prospect of three-dimensional crystals is poor. By combining neutron and X-ray fiber diffraction, NMR, circular dichroism, and Raman and infrared spectroscopies, an atomic model for the filamentous bacteriophage Pfl has been derived (Liu and Day, 1994). Other studies concerning Pfl have relied on purely X-ray fiber diffraction data, together with molecular modeling, to provide detailed filament structures (Pederson et at, 2001 Welsh et at, 1998a,b, 2000). Eiber diffraction was also used to solve the structure of the rodlike helical tobacco mosaic virus (TMV), where all of the coat protein and three genomic nucleotides... 

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