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BACKGROUND The actin-binding site of several cytoskeletal proteins is comprised of two calponin homology (CH) domains in a tandem arrangement. As a single copy, the CH domain is also found in regulatory proteins in muscle and in signal-transduction proteins. The three-dimensional structures of three CH domains are known, but they have not yet clarified the(More)
SAD data on a triiodide derivative of porcine pancreatic elastase have been recorded from a single sample using 2.0 A wavelength X-rays. The large anomalous signal of iodine at this wavelength allowed the detection of heavy-atom sites and subsequent structure determination using low-redundancy data. Substantial radiation damage was observed during the(More)
Alpha-actinin is the major F-actin crosslinking protein in both muscle and non-muscle cells. We report the crystal structure of the actin binding domain of human muscle alpha-actinin-3, which is formed by two consecutive calponin homology domains arranged in a "closed" conformation. Structural studies and available biochemical data on actin binding domains(More)
The majority of 3D structures of macromolecules are currently determined by macromolecular crystallography, which employs the diffraction of X-rays on single crystals. However, during diffraction experiments, the X-rays can damage the protein crystals by ionization processes, especially when powerful X-ray sources at synchrotron facilities are used. This(More)
Superoxide dismutases (SODs, EC 1.15.1.1) are ubiquitous enzymes that efficiently catalyze the dismutation of superoxide radical anions to protect biological molecules from oxidative damage. The crystal structure of nickel-containing SOD (NiSOD) from Streptomyces seoulensis was determined for the resting, x-ray-reduced, and thiosulfate-reduced enzyme state.(More)
Binding of the human recombinant secretory leukocyte proteinase inhibitor (SLPI) [native and with the methionyl residues at positions 73, 82, 94 and 96 of domain 2 oxidized to the sulfoxide derivative (Met(O) SLPI)] to bovine alpha-chymotrypsin (alpha-chymotrypsin) [native and with the Met192 residue converted to the sulfoxide derivative (Met(O)(More)
Superoxide dismutases are metalloenzymes which catalyse the disproportion of superoxide radicals and thus play an important role in the protection of biomolecules from oxidative damage. Redox-active metal ions known to act as the catalytic centre of these enzymes are Cu, Mn or Fe. Recently, enzymes containing Ni have been found in various Streptomyces(More)
Human gamma-filamin is a protein of 2705 amino-acid residues that localizes mainly in the myofibrillar Z-disc and to smaller extent in the subsarcolemmal region of striated muscle cells. gamma-Filamin consists of an N-terminal actin-binding domain followed by a long rod-shaped region. The rod-shaped region consists of 24 immunoglobulin-like domains that(More)
Filamin C is a dimeric, actin-binding protein involved in organization of cortical cytoskeleton and of the sarcomere. We performed crystallographic, small-angle X-ray scattering and analytical ultracentrifugation experiments on the constructs containing carboxy-terminal domains of the protein (domains 23-24 and 19-21). The crystal structure of domain 23 of(More)