W
Wojciech Rypniewski
Researcher at Polish Academy of Sciences
Publications - 103
Citations - 5606
Wojciech Rypniewski is an academic researcher from Polish Academy of Sciences. The author has contributed to research in topics: Active site & Crystal structure. The author has an hindex of 29, co-authored 98 publications receiving 5240 citations. Previous affiliations of Wojciech Rypniewski include European Bioinformatics Institute & Bulgarian Academy of Sciences.
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Journal ArticleDOI
Three-dimensional structure of myosin subfragment-1: a molecular motor
Ivan Rayment,Wojciech Rypniewski,Karen Schmidt-Bäse,Karen Schmidt-Bäse,Robert Smith,Diana R. Tomchick,Diana R. Tomchick,Matthew M. Benning,Donald A. Winkelmann,Gary E. Wesenberg,Hazel M. Holden +10 more
TL;DR: The three-dimensional structure of the head portion of myosin, or subfragment-1, which contains both the actin and nucleotide binding sites, is described, and this structure of a molecular motor was determined by single crystal x-ray diffraction.
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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.
Stefano Benini,Wojciech Rypniewski,Keith S. Wilson,Silvia Miletti,Stefano Ciurli,Stefano Mangani +5 more
TL;DR: The mode of binding of the inhibitor, and a comparison between the native and inhibited urease structures, indicate a novel mechanism for enzymatic urea hydrolysis which reconciles the available structural and biochemical data.
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The molecular structure of insecticyanin from the tobacco hornworm Manduca sexta L. at 2.6 A resolution.
TL;DR: Interestingly the overall three‐dimensional fold of the insecticyanin subunit shows remarkable similarity to the structural motifs of bovine beta‐lactoglobulin and the human serum retinol‐binding protein.
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High-resolution native and complex structures of thermostable β-mannanase from Thermomonospora fusca – substrate specificity in glycosyl hydrolase family 5
Mark Hilge,Sergio M. Gloor,Wojciech Rypniewski,Oliver Sauer,Tom D Heightman,Wolfgang Zimmermann,Kaspar H. Winterhalter,Klaus Piontek +7 more
TL;DR: It is proposed that selectivity arises from two possible mechanisms: a hydrophobic interaction of the substrate with Val263, conserved in family 5 bacterial mannanases, which discriminates between the different conformations of the hydroxymethyl group in native mannan and cellulose; and/or a specific interaction between Asp259 and the axial hydroxyl group at the C(2) of the substrates in the -2 subsite.
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Structural properties of the nickel ions in urease: novel insights into the catalytic and inhibition mechanisms
Stefano Ciurli,Stefano Benini,Wojciech Rypniewski,Keith S. Wilson,Silvia Miletti,Stefano Mangani +5 more
TL;DR: In this article, a comprehensive critical summary of urease spectroscopy, crystallography, inhibitor binding, and site-directed mutagenesis, with special emphasis given to the relationships between the structural features of the Ni-containing active site and the physico-chemical and biochemical properties of this metallo-enzyme.