M
Miroslaw Cygler
Researcher at University of Saskatchewan
Publications - 201
Citations - 14729
Miroslaw Cygler is an academic researcher from University of Saskatchewan. The author has contributed to research in topics: Active site & Binding site. The author has an hindex of 58, co-authored 199 publications receiving 14066 citations. Previous affiliations of Miroslaw Cygler include National Research Council & National Republican Congressional Committee.
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Journal ArticleDOI
The α/β hydrolase fold
David L. Ollis,Eong Cheah,Miroslaw Cygler,Bauke W. Dijkstra,Felix Frolow,Sybille M. Franken,Michal Harel,S. Jamse Remington,Israel Silman,Joseph D. Schrag,Joel L. Sussman,Koen H. G. Verschueren,Adrian Goldman +12 more
TL;DR: The alpha/beta hydrolase fold as mentioned in this paper is common to several hydrolytic enzymes of widely differing phylogenetic origin and catalytic function, including the serine protease catalytic triad.
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Bacillus thuringiensis CryIA(a) insecticidal toxin: crystal structure and channel formation.
Pawel Grochulski,Luke Masson,Svetlana Borisova,Marianne Pusztai-Carey,Jean-Louis Schwartz,Roland Brousseau,Miroslaw Cygler +6 more
TL;DR: Comparison with the structure of CryIIIA, a coleopteran-specific toxin, shows that although the fold of these two proteins is similar, there are significant structural differences within domain II, which supports the conclusions from genetic studies that domain II is involved in recognition and binding to cell surface receptors.
Journal ArticleDOI
Relationship between sequence conservation and three‐dimensional structure in a large family of esterases, lipases, and related proteins
Miroslaw Cygler,Joseph D. Schrag,Joel L. Sussman,Michal Harel,Israel Silman,Mary K. Gentry,Bhupendra P. Doctor +6 more
TL;DR: An improved alignment of a collection of 32 related amino acid sequences of other esterases, lipases, and related proteins was obtained, and 24 residues are found to be invariant in 29 sequences of hydrolytic enzymes, and an additional 49 are well conserved.
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Insights into interfacial activation from an open structure of Candida rugosa lipase.
Pawel Grochulski,Yunge Li,Joseph D. Schrag,Francois Bouthillier,P. Smith,D. Harrison,B. Rubin,Miroslaw Cygler +7 more
TL;DR: The structure of the Candida rugosa lipase determined at 2.06-A resolution reveals a conformation with a solvent-accessible active site and provides a new image of the substrate binding region and active site access, which is different from that inferred from theructure of the "closed" form of the G. candidum lipase.
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Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum
TL;DR: The three-dimensional structure of a lipase from G. candidum is reported at 2.2 Å resolution, and the catalytic triad of GCL is Ser-His-Glu, with glutamic acid replacing the usual aspartate.