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Structural characterization of O- and C-glycosylating variants of the landomycin glycosyltransferase LanGT2.


ABSTRACT: The structures of the O-glycosyltransferase LanGT2 and the engineered, C-C bond-forming variant LanGT2S8Ac show how the replacement of a single loop can change the functionality of the enzyme. Crystal structures of the enzymes in complex with a nonhydrolyzable nucleotide-sugar analogue revealed that there is a conformational transition to create the binding sites for the aglycon substrate. This induced-fit transition was explored by molecular docking experiments with various aglycon substrates.

SUBMITTER: Tam HK 

PROVIDER: S-EPMC4376353 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature

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Structural characterization of O- and C-glycosylating variants of the landomycin glycosyltransferase LanGT2.

Tam Heng Keat HK   Härle Johannes J   Gerhardt Stefan S   Rohr Jürgen J   Wang Guojun G   Thorson Jon S JS   Bigot Aurélien A   Lutterbeck Monika M   Seiche Wolfgang W   Breit Bernhard B   Bechthold Andreas A   Einsle Oliver O  

Angewandte Chemie (International ed. in English) 20150107 9


The structures of the O-glycosyltransferase LanGT2 and the engineered, C-C bond-forming variant LanGT2S8Ac show how the replacement of a single loop can change the functionality of the enzyme. Crystal structures of the enzymes in complex with a nonhydrolyzable nucleotide-sugar analogue revealed that there is a conformational transition to create the binding sites for the aglycon substrate. This induced-fit transition was explored by molecular docking experiments with various aglycon substrates. ...[more]

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