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  • 1
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-1432
    Keywords: Protein structure ; Lysozyme ; Structural correspondence ; Divergent evolution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The three-dimensional structure of goose-type lysozyme (GEWL), determined by x-ray crystallography and refined at high resolution, has similarities to the structures of hen (chicken) eggwhite lysozyme (HEWL) and bacteriophage T4 lysozyme (T4L). The nature of the structural correspondence suggests that all three classes of lysozyme diverged from a common evolutionary precursor, even though their amino acid sequences appear to be unrelated (Grütter et al. 1983). In this paper we make detailed comparisons of goose-type, chicken-type, and phage-type lysozymes. The lysozymes have undergone conformational changes at both the blobal and the local level. As in the globins, there are corresponding α-helices that have rigid-body displacements relative to each other, but in some cases corresponding helices have increased or decreased in length, and in other cases there are helices in one structure that have no counterpart in another. Independent of the overall structural correspondence among the three lysozyme backbones is another, distinct correspondence between a set of three consecutive α-helices in GEWL and three consecutive α-helices in T4L. This structural correspondence could be due, in part, to a common energetically favorable contact between the first and the third helices. There are similarities in the active sites of the three lysozymes, but also one striking difference. Glu 73 (GEWL) spatially corresponds to Glu 35 (HEWL) and to Glu 11 (T4L). On the other hand, there are two aspartates in the GEWL active site, Asp 86 and Asp 97, neither of which corresponds exactly to Asp 52 (HEWL) or Asp 20 (T4L). (The discrepancy in the location of the carboxyl groups is about 10 Å for Asp 86 and 4 Å for Asp 97.) This lack of structural correspondence may reflect some differences in the mechanisms of action of three lysozymes. When the amino acid sequences of the three lysozyme types are aligned according to their structural correspondence, there is still no apparent relationship between the sequences except for possible weak matching in the vicinity of the active sites.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 50 (1994), S. 85-92 
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Transforming growth factor-β is a multifunctional cell-growth regulator and is a member of the TGF-β superfamily of cytokines. Each monomer is 112 amino acids long and the mature active form is a 25 kDa homodimer. Recently, the crystal structure of TGF-β2 has been determined independently in two laboratories [Daopin, Piez, Ogawa & Davies (1992). Science, 257, 369–373; Schlunegger & Grütter (1992). Nature (London), 358, 430–434] and subsequently refined to higher resolutions [Daopin, Li & Davies (1993). Proteins Struct. Funct. Genet. In the press; Schlunegger & Grütter (1993). J. Mol. Biol. In the press]. A detailed structural comparison shows that the two structures are nearly identical with the differences mostly located on the mobile regions of the molecule. The r.m.s. differences between the two structures are 0.10 Å for 104 pairs of Cα atoms, 0.15 Å for 434 pairs of main-chain atoms, 0.33 Å for 860 out of 890 pairs of protein atoms and a correlation of 90% between the temperature B factors of all protein atoms. Based on a comparison of the water molecules, a B value of 60.0 Å2 is recommended as the cut off for modeling new waters. The structural identity is striking because in one case the material was expressed in vivo in CHO cells whereas in the other case it was expressed in E. coli and had to be refolded in vitro. The overall coordinate errors are estimated to be 0.21 Å from the Luzzati plot, 0.18 Å from the σA plot, 0.24 Å with Cruickshank's equations and 0.25 Å using the empirical method of Perry & Stroud. These estimates are comparable to the r.m.s. structure superposition. The r.m.s. differences correlate very well with the crystallographic B values and the relation is best described with the Cruickshank formula. In addition to the estimation of an overall error, a new application of the Cruickshank formula is presented here to estimate the local errors.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    [S.l.] : International Union of Crystallography (IUCr)
    Acta crystallographica 37 (1981), S. 701-710 
    ISSN: 1600-5724
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: An oscillation data collection system for protein crystallography is described. The system consists of a modified Enraf-Nonius precession camera with cylindrical cassette, and stepping motor driven by a flexible microprocessor control system. The X-ray source is graphite-monochromatized radiation from an Elliott GX-21 rotating-anode generator run at 5.5 kW on a focal spot measuring 0.5 × 5.0 mm. The potential advantages of using a relatively large focal spot in conjunction with a graphite monochromator are discussed. Conditions for optimum collimation and X-ray intensity are considered, and it is shown that appropriately designed collimators with adjustable apertures can have substantial advantages over commercially available pinhole collimators. The oscillation films are processed by a procedure based on that of Rossmann [J. Appl. Cryst. (1979), 12, 225-238]. Determination of the initial alignment of the film is facilitated by a pair of reference pins incorporated in the cylindrical cassette. These pins ensure that the position of the film in the cassette is known, and avoid the need for fiducial marks. The crystal alignment and film measurement technique is fully automatic, requiring no prior input other than the approximate starting orientation of the crystal, the approximate unit-cell dimensions, and the angular oscillation range. An alternative method for the determination of crystal orientation is proposed which has been found to be somewhat superior to that of Rossmann, especially for smaller unit cells.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 53 (1997), S. 224-226 
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Purified recombinant membrane apoprotein cyclooxygenase-2 (COX-2) has been reconstituted with heme and characterized. The holoprotein has been crystallized in complex with the selective inhibitor CGP 28238 [6-(2,4-difluorophenoxy)-5- methylsulfonylamino-l-indanone] by the sitting-drop method of vapor diffusion using polyethylene glycol 2000 monomethyl ether as precipitant, in the presence of the nonionic detergent β-octylglucoside. The crystals are orthorhombic, belonging to the space group P21212 with cell dimensions a = 209.56, b = 71.28 and c = 93.82 Å, and diffract to 2.5 Å resolution. The asymmetric unit contains two COX-2 monomers, as confirmed by the molecular replacement solution and in agreement with the dimeric structure of the detergent-solubilized protein found with dynamic light scattering and size-exclusion chromatography. Structural work is in progress.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 290 (1981), S. 334-335 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] If anything, the large number of protein structures and amino acid sequences now known has confused rather than simplified the main issue of whether extant proteins have evolved from a small number of ancestral precursors or have arisen independently. When the amino acid sequences are closely ...
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 303 (1983), S. 828-831 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The structure determination of goose lysozyme14 by isomor-phous replacement1'15 was based on four heavy-atom replace ments supplemented by an additional data set collected16'17 for one of the derivatives at lower substitution. Electron density maps calculated at 2.8 A and 3.2 A resolution showed ...
    Type of Medium: Electronic Resource
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