8IXP

Apo structure of glycosyltransferase LmbT wild type

8IXP の概要

• エントリーDOI: 10.2210/pdb8ixp/pdb
• 分子名称: Glycosyltransferase (2 entities in total)
• 機能のキーワード: lincomycin, glycosyltransferase, biosynthesis, transferase
• 由来する生物種: Streptomyces lincolnensis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 195636.66

構造登録者

Mori, T.,Sun, X.,Abe, I. (登録日: 2023-04-02, 公開日: 2024-04-03, 最終更新日: 2024-10-30)

主引用文献

Mori, T.,Sun, X.,Kadlcik, S.,Janata, J.,Abe, I.
Structure-Function Analysis of the S-Glycosylation Reaction in the Biosynthesis of Lincosamide Antibiotics.
Angew.Chem.Int.Ed.Engl., 62:e202304989-e202304989, 2023

PubMed Abstract: The S-glycosyltransferase LmbT, involved in the biosynthesis of lincomycin A, is the only known enzyme that catalyzes the enzymatic incorporation of rare amino acid L-ergothioneine (EGT) into secondary metabolites. Here, we show the structure and function analyses of LmbT. Our in vitro analysis of LmbT revealed that the enzyme shows promiscuous substrate specificity toward nitrogenous base moieties in the generation of unnatural nucleotide diphosphate (NDP)-D-α-D-lincosamides. Furthermore, the X-ray crystal structures of LmbT in its apo form and in complex with substrates indicated that the large conformational changes of the active site occur upon binding of the substrates, and that EGT is strictly recognized by salt-bridge and cation-π interactions with Arg260 and Trp101, respectively. The structure of LmbT in complex with its substrates, the docking model with the EGT-S-conjugated lincosamide, and the structure-based site-directed mutagenesis analysis revealed the structural details of the LmbT-catalyzed S 2-like S-glycosylation reaction with EGT.

PubMed: 37222528
DOI: 10.1002/anie.202304989

実験手法

X-RAY DIFFRACTION (2.45 Å)