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Structure of formylglycine-generating enzyme in complex with copper and a substrate reveals an acidic pocket for binding and activation of molecular oxygen
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 4527759
Author(s) Miarzlou, Dzmitry A.; Leisinger, Florian; Joss, Daniel; Häussinger, Daniel; Seebeck, Florian P.
Author(s) at UniBasel Seebeck, Florian Peter
Häussinger, Daniel
Year 2019
Title Structure of formylglycine-generating enzyme in complex with copper and a substrate reveals an acidic pocket for binding and activation of molecular oxygen
Journal Chemical Science
Volume 10
Number 29
Pages / Article-Number 7049-7058
Abstract The formylglycine generating enzyme (FGE) catalyzes oxidative conversion of specific peptidyl-cysteine residues to formylglycine. FGE mediates O; 2; -activation and hydrogen-atom abstraction in an active site that contains Cu(i) coordinated to two cysteine residues. Similar coordination geometries are common among copper-sensing transcription factors and copper-chaperone but are unprecedented among copper-dependent oxidases. To examine the mechanism of this unusual catalyst we determined the 1.04 Å structure of FGE from; Thermomonospora curvata; in complex with copper and a cysteine-containing peptide substrate. This structure unveils a network of four crystallographic waters and two active site residues that form a highly acidic O; 2; -binding pocket juxtaposed to the trigonal planar tris-cysteine coordinated Cu(i) center. Comparison with structures of FGE in complex with Ag(i) and Cd(ii) combined with evidence from NMR spectroscopy and kinetic observations highlight several structural changes that are induced by substrate binding and prime the enzyme for O; 2; -binding and subsequent activation.
Publisher Royal Society of Chemistry
ISSN/ISBN 2041-6520 ; 2041-6539
edoc-URL https://edoc.unibas.ch/75096/
Full Text on edoc Available
Digital Object Identifier DOI 10.1039/c9sc01723b
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/31588272
ISI-Number 000476912600009
Document type (ISI) Journal Article
 
   

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05/05/2024