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- Bernier-Villamor, V, et al.
(author)
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Crystallization and preliminary X-ray diffraction of Trypanosoma cruzi dUTPase
- 1999
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In: Acta Crystallographica. Section D: Biological Crystallography. - 1399-0047. ; D55, s. 528-530
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Journal article (peer-reviewed)abstract
- Crystals of Trypanosoma cruzi dUTPase have been grown. Two different morphologies are observed, depending on the molecular weight of the PEG used as precipitating agent in the mother liquor, both having a hexagonal unit cell with similar dimensions. Complete X-ray diffraction data have been collected to low resolution for one of the forms. The space group is P6322, with unit-cell dimensions a = 134.15, c = 147.05 Å. Peaks in the self-rotation function and the solvent content are consistent with two molecules of dUTPase per asymmetric unit.
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- Chaudhuri, BN, et al.
(author)
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Structures of cellular retinoic acid binding proteins I and II in complex with synthetic retinoids
- 1999
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In: ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY. - 0907-4449. ; 55, s. 1850-1857
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Journal article (peer-reviewed)abstract
- Retinoids play important roles in diverse cellular processes including growth, cell differentiation and vision. Many natural and synthetic retinoids are used as drugs in dermatology and oncology. A large amount of data has been accumulated on the cellular activity of different synthetic retinoids. They are stabilized and transported inside the cell cytoplasm by binding and transport proteins, such as cellular retinol-binding proteins and cellular retinoic acid binding proteins (CRABPs). The structures of human CRABP II in complex with two different synthetic retinoids, Ro13-6307 and Ro12--7310 (at 2.1 and 2.0 A resolution, respectively) and of bovine CRABP I in complex with a retinobenzoic acid, Am80 (at 2.8 A resolution) are described. The binding affinities of human CRABP I and II for the retinoids studied here have been determined. All these compounds have comparable binding affinities (nanomolar range) for both CRABPs. Apart from the particular interactions of the carboxylate group of the retinoids with specific protein groups, each structure reveals characteristic interactions. Studying the atomic details of the interaction of retinoids with retinoid-binding proteins facilitates the understanding of the kinetics of retinoid trafficking inside the cytoplasm.
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- Chaudhuri, BN, et al.
(author)
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The structures of alpha(2u)-globulin and its complex with a hyaline droplet inducer
- 1999
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In: ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY. - 0907-4449. ; 55, s. 753-762
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Journal article (peer-reviewed)abstract
- Alpha 2u-globulin (A2U) is the major urinary protein excreted by adult male rats. The structure of a monoclinic crystal form of A2U was reported in 1992 [Bocskei et al. (1992). Nature (London), 360, 186-188]. The structures of an orthorhombic crystal form of A2U at 2. 5 A resolution (refined to an R factor of 0.248; Rfree = 0.264) and of a complex between A2U and d-limonene 1,2-epoxide (DLO) at 2.9 A resolution (R factor = 0.248; Rfree = 0.260) are presented here. DLO is one of a diverse group of chemicals which cause a male rat-specific renal carcinogenesis called hyaline-droplet nephropathy. The rate-determining step in the development of this disorder is the binding of the toxin to A2U. Comparison of the cavities in A2U and in the corresponding mouse urinary protein (MUP) reveal that the former is tailor-made for small oval hydrophobic ligands such as DLO. The cavity in MUP is more shallow and elongated and cannot easily accommodate such ligands.
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- Dauter, Z, et al.
(author)
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The Refined Structure of dUTPase from Escherichia coli
- 1998
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In: Acta Crystallographica. Section D: Biological Crystallography. - 1399-0047. ; D54:5, s. 735-749
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Journal article (peer-reviewed)abstract
- Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase, E.C. 3.6.1.23) catalyzes the hydrolysis of dUTP to dUMP and pyrophosphate and is involved in nucleotide metabolism and DNA synthesis. A crystal of the recombinant E. coli enzyme, precipitated from polyethylene glycol mixtures in the presence of succinate at pH 4.2, was used to collect synchrotron diffraction data to 1.9 Å resolution, in space group R3, a = b = 86.62, c = 62.23 Å. Mercury and platinum derivative data were collected at wavelengths to optimize the anomalous contribution. The resulting 2.2 Å MIRAS phases differed from the final set by 40° on average and produced an excellent map which was easy to interpret. The model contains 132 water molecules and refined to an R value of 13.7%. 136 residues have clear electron density out of 152 expected from the gene sequence. The 16 C-terminal residues are presumably disordered in the crystal lattice. The monomer is a `jelly-roll' type, containing mostly -sheet and only one short helix. The molecule is a tight trimer. A long C-terminal arm extends from one subunit and encompasses the next one within the trimer contributing to its -sheet. Conserved sequence motifs common among dUTPases, previously suggested to compose the active site and confirmed in a recent study of the dUDP complex, are located at subunit-subunit interfaces along the threefold axis, in parts of the -sheet and in loop regions. A similar molecular architecture has recently been found in two other trimeric dUTPases.
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