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Two different crystal forms of sorcin, a penta-EF-hand Ca2+-binding protein (2001)

Nastopoulos, Vassilios ; Ilari, Andrea ; Colotti, Gianni ; [et al.]

Copenhagen : International Union of Crystallography (IUCr)

Acta crystallographica 57 (2001), S. 862-864

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ISSN: 1399-0047

Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001

Topics: Chemistry and Pharmacology , Geosciences , Physics

Notes: Sorcin is a 198 amino-acid Ca2+-binding protein that belongs to the penta-EF-hand family. Its Ca2+-binding domain (residues 33–198) has been crystallized in the absence of Ca2+ in two different crystal forms. Two complete data sets have been collected on a synchrotron source under cryocooling conditions from crystals grown using ammonium sulfate as precipitant: monoclinic crystals in space group C2, with unit-cell parameters a = 130.93, b = 103.85, c = 78.55 Å, β = 118.0°, diffracting to 2.1 Å, and tetragonal crystals in space group P4212, with unit-cell parameters a = b = 103.33, c = 79.15, diffracting to 2.7 Å. Crystals were also grown using PEG 6000 as precipitating agent. They also belong to space group C2, diffract to 2.8 Å and their unit-cell parameters are very similar to the first form. Structure determination by molecular replacement has been initiated. Structural information should be useful for elucidating the interaction of sorcin with membrane targets.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1107/S0907444901004553

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Interaction of lactoferrin with Escherichia coli cells and correlation with antibacterial activity (1990)

Visca, Paolo ; Dalmastri, Claudia ; Verzili, Daniela ; [et al.]

Springer

Medical microbiology and immunology 179 (1990), S. 323-333

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ISSN: 1432-1831

Source: Springer Online Journal Archives 1860-2000

Topics: Medicine

Notes: Abstract It has been established that the antimicrobial activity of lactoferrin towards Escherichia coli is enhanced by a direct contact between the protein and the microbial cell and that, in the case of E. coli K-12 strains, an antibacterial activity of lactoferrin unrelated to iron withdrawal is present. Evidence is now reported that lactoferrin binds to surface structures expressed in E. coli K-12 strains grown in either an “excess” or “stress” of iron. Under the experimental conditions used, lactoferrin binding both in the apo and in the iron-saturated form yields a maximum of 1.6 × 105 bound molecules/E. coli K-12 cell; the amount of lactoferrin bound does not depend on the expression of the iron-regulated outer membrane proteins. In contrast, lactoferrin does not bind to E. coli clinical isolates. Apo-lactoferrin (at 500 μ/ml in a chemically defined medium) inhibits the growth of E. coli K-12 strains but not of clinical isolates. These findings suggest that the antibacterial activity of the protein could be associated to its binding to the cell surface.