Illuminating the mechanism and allosteric behavior of NanoLuc luciferase
Illuminating the mechanism and allosteric behavior of NanoLuc luciferase
About this item
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Author / Creator
Nemergut, Michal , Pluskal, Daniel , Horackova, Jana , Sustrova, Tereza , Tulis, Jan , Barta, Tomas , Baatallah, Racha , Gagnot, Glwadys , Novakova, Veronika , Majerova, Marika , Sedlackova, Karolina , Marques, Sérgio M. , Toul, Martin , Damborsky, Jiri , Prokop, Zbynek , Bednar, David , Janin, Yves L. and Marek, Martin
Publisher
London: Nature Publishing Group UK
Journal title
Language
English
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Publication information
Publisher
London: Nature Publishing Group UK
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Scope and Contents
Contents
NanoLuc, a superior β-barrel fold luciferase, was engineered 10 years ago but the nature of its catalysis remains puzzling. Here experimental and computational techniques are combined, revealing that imidazopyrazinone luciferins bind to an intra-barrel catalytic site but also to an allosteric site shaped on the enzyme surface. Structurally, binding...
Alternative Titles
Full title
Illuminating the mechanism and allosteric behavior of NanoLuc luciferase
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Primary Identifiers
Record Identifier
TN_cdi_doaj_primary_oai_doaj_org_article_02510bf81fd243d0bfed12a6fdc366d5
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_02510bf81fd243d0bfed12a6fdc366d5
Other Identifiers
ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-023-43403-y
