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Three-dimensional structure of myosin subfragment-1: a molecular motor.
Directed movement is a characteristic of many living organisms and occurs as a result of the transformation of chemical energy into mechanical energy. Myosin is one of three families of molecularExpand
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Evolutionary divergence and conservation of trypsin.
The trypsin sequences currently available in the data banks have been collected and aligned using first the amino acid sequence homology and, subsequently, the superposed crystal structures ofExpand
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A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis costs two nickels.
BACKGROUND Urease catalyzes the hydrolysis of urea, the final step of organic nitrogen mineralization, using a bimetallic nickel centre. The role of the active site metal ions and amino acid residuesExpand
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Structural properties of the nickel ions in urease: novel insights into the catalytic and inhibition mechanisms
Abstract This work provides a comprehensive critical summary of urease spectroscopy, crystallography, inhibitor binding, and site-directed mutagenesis, with special emphasis given to theExpand
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The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 Å resolution
Abstract The structure of Bacillus pasteurii urease inhibited with acetohydroxamic acid was solved and refined anisotropically using synchrotron X-ray cryogenic diffraction data (1.55 Å resolution,Expand
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Structure-based rationalization of urease inhibition by phosphate: novel insights into the enzyme mechanism
Abstract. The structure of Bacilluspasteurii urease (BPU) inhibited with phosphate was solved and refined using synchrotron X-ray diffraction data from a vitrified crystal (1.85 Å resolution, 99.3%Expand
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Molecular details of urease inhibition by boric acid: insights into the catalytic mechanism.
The structure of the complex of urease, a Ni-containing metalloenzyme, with boric acid was determined at 2.10 A resolution. The complex shows the unprecedented binding mode of the competitiveExpand
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The sequence and X-ray structure of the trypsin from Fusarium oxysporum.
The trypsin from Fusarium oxysporum is equally homologous to trypsins from Streptomyces griseus, Streptomyces erythraeus and to bovine trypsin. A DFP (diisopropylfluorophosphate) inhibited form ofExpand
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The complex of Bacillus pasteurii urease with β-mercaptoethanol from X-ray data at 1.65-Å resolution
Abstract The structure of β-mercaptoethanol-inhibited urease from Bacillus pasteurii, a highly ureolytic soil micro-organism, was solved at 1.65 Å using synchrotron X-ray cryogenic diffraction data.Expand
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Structural consequences of reductive methylation of lysine residues in hen egg white lysozyme: an X-ray analysis at 1.8-A resolution.
Chemical modification of proteins has been and continues to be an important biochemical tool for the study of protein structure and function. One such type of approach has been the reductiveExpand
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