1,720,981 research outputs found
Crystallization and preliminary X-ray crystallographic analysis of the unusual ferritin from Listeria innocua
Full text linkSingle crystals of ferritin extracted from Listeria innocua have been obtained by the vapour-diffusion method using PEG 1000 as precipitant. The crystals are orthorhombic, space group P212121, with unit-cell dimensions a = 87.7, b = 137.5, c = 173.1 Å. The crystals diffract to 2.9 Å resolution on a rotating-anode X-ray source and to 2.35 Å resolution on a synchrotron X-ray source. The asymmetric unit contains one molecule formed by 12 subunits, corresponding to a packing density of 2.41 Å3 Da-1
The dodecameric ferritin fron Listeria innocua contains a novel intersubunit iron-binding site
No full textCrystallization and x-ray diffraction measurements of a themophilic archaeal recombinant amidase from Sulfolobus sofataricus MT4
No full textRecombinant amidase is a 55.8 kDa enzyme from the thermophilic archaeon Sulfolobus solfataricus MT4 that catalyses the hydrolysis of aliphatic amides of 2-6 C atoms as well as many aromatic amides. Single crystals of purified amidase were obtained by the hanging-drop method at 294 K. Diffraction data for the native protein (2.55 A resolution) and a putative derivative (2.20 A) have been collected at low temperature using synchrotron radiation. The crystals belong to the rhombohedral space group R3. Structure determination by multiple isomorphous replacement is in progress. It is expected that structural information from this signatured thermostable amidase will increase our knowledge of the molecular mechanisms employed to maintain high-temperature stability in thermophilic proteins
The crystal structure of saporin SO6 from Saponaria officinalis and its interaction with the ribosome
No full textThe 2.0 Angstrom resolution crystal structure of the ribosome inactivating protein saporin (isoform 6) from seeds of Saponaria officinalis is presented. The fold typical of other plant toxins is conserved, despite some differences in the loop regions. The loop between strands beta 7 and beta 8 in the C-terminal region which spans over the active site cleft appears shorter in saporin, suggesting an easier access to the substrate. Furthermore,ve investigated the molecular interaction between saporin and the yeast ribosome by differential chemical modifications. A contact surface inside the C-terminal region of saporin has been identified. Structural comparison between saporin and other ribosome inactivating proteins reveals that this region is conserved and represents a peculiar motif involved in ribosome recognition. (C) 2000 Federation of European Biochemical Societies
Crystallization and preliminary X-ray study of Saporin, a Ribosome Inactivating Protein from Saponaria officinalis
No full textSingle crystals of the protein saporin isolated from the seeds of S. officinalis have been grown by the vapor-diffusion method using ammonium sulfate as precipitant. The crystals are tetragonal, space group P4(1)22 (P4(3)22), with cell-dimensions a = b = 67.53 and c = 119.67 Angstrom, and diffract to 2.0 Angstrom resolution on a rotating-anode X-ray source. The asymmetric unit contains one molecule, corresponding to a volume of the asymmetric unit per unit mass (V-m) of 2.38 Angstrom(3) Da(-1)
Structural requirements of endopolygalacturonase for the interaction with PGIP (polygalacturonase-inhibiting protein)
No full textTo invade a plant tissue, phytopathogenic fungi produce several cell wall-degrading enzymes; among them, endopolygalacturonase (PG) catalyzes the fragmentation and solubilization of homogalacturonan. Polygalacturonase-inhibiting proteins (PGIPs), found in the cell wall of many plants, counteract fungal PGs by forming specific complexes with them. We report the crystal structure at 1.73 Angstrom resolution of PG from the phytopathogenic fungus Fusarium, moniliforme (FmPG). The structure of FmPG was useful to study the mode of interaction of the enzyme with PGIP-2 from Phaseolus vulgaris. Several amino acids of FmPG were mutated, and their contribution to the formation of the complex with PGIP-2 was investigated by surface plasmon resonance. The residues Lys-269 and Arg-267, located inside the active site cleft, and His-188, at the edge of the active site cleft, are critical for the formation of the complex, which is consistent with the observed competitive inhibition of the enzyme played by PGIP-2. The replacement of His-188 with a proline or the insertion of a tryptophan after position 270, variations that both occur in plant PGs, interferes with the formation of the complex. We suggest that these variations are important structural requirements of plant PGs to prevent PGIP binding
Crystallization and preliminary X-ray diffraction study of the endopolygalacturonase from Fusarium moniliforme
No full textCrystal structure of the complex between pectin methylesterase and pectin methylesterase inhibitor
No full textStructural view of the complex between pectin methylesterase and pectin methylesterase inhibitor
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