E
Emil F. Pai
Researcher at University of Toronto
Publications - 203
Citations - 15866
Emil F. Pai is an academic researcher from University of Toronto. The author has contributed to research in topics: Binding site & Xanthine dehydrogenase. The author has an hindex of 58, co-authored 203 publications receiving 14840 citations. Previous affiliations of Emil F. Pai include Toronto General Hospital & University of Georgia.
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Journal ArticleDOI
Insights into ligand binding and catalysis of a central step in NAD+ synthesis: structures of Methanobacterium thermoautotrophicum NMN adenylyltransferase complexes.
Vivian Saridakis,Vivian Saridakis,Dinesh Christendat,Dinesh Christendat,Matthew S. Kimber,Akil Dharamsi,Aled M. Edwards,Emil F. Pai +7 more
TL;DR: The structure of Methanobacterium thermoautotrophicum NMNATase determined using multiwavelength anomalous dispersion phasing revealed a nucleotide-binding fold common to nucleotidyltransferase proteins, allowing the identification of residues involved in product binding.
Journal ArticleDOI
Protein conformational gating of enzymatic activity in xanthine oxidoreductase
Hiroshi Ishikita,Bryan T. Eger,Ken Okamoto,Takeshi Nishino,Takeshi Nishino,Takeshi Nishino,Emil F. Pai,Emil F. Pai +7 more
TL;DR: The majority of the E(sq/hq) difference between XDH and XO originates from a conformational change in the loop at positions 423-433 near the flavin binding site, causing the differences in stability of the semiquinone state.
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The crystal structure of (S)-3-O-geranylgeranylglyceryl phosphate synthase reveals an ancient fold for an ancient enzyme
TL;DR: An early evolutionary history for AfGGGPS is postulated, which may highlight its role in the emergence of Archaea and proposed functions for the homologous PcrB proteins, which are conserved in a subset of pathogenic bacteria, as either prenyltransferases or being involved in lipoteichoic acid biosynthesis.
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Hydrophobic Gating of Ion Permeation in Magnesium Channel CorA.
TL;DR: Findings support an allosteric mechanism whereby wetting of a hydrophobic gate couples changes in intracellular magnesium concentration to the onset of ionic conduction.
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X-ray Structure of a Hg2+ Complex of Mercuric Reductase (MerA) and Quantum Mechanical/Molecular Mechanical Study of Hg2+ Transfer between the C-Terminal and Buried Catalytic Site Cysteine Pairs
Peng Lian,Hao-Bo Guo,Hao-Bo Guo,Demian Riccardi,Demian Riccardi,Aiping Dong,Jerry M. Parks,Qin Xu,Emil F. Pai,Emil F. Pai,Susan M. Miller,Dong-Qing Wei,Jeremy C. Smith,Jeremy C. Smith,Hong Guo,Hong Guo +15 more
TL;DR: The transfer of this soft divalent cation is found to be nearly thermoneutral and to pass through a stable tricoordinated intermediate that is marginally less stable than the two end states.