5T39

Crystal Structure of the N-terminal domain of EvdMO1 in the presence of SAH and D-fucose

5T39 の概要

• エントリーDOI: 10.2210/pdb5t39/pdb
• 関連するPDBエントリー: 5T38
• 分子名称: EvdMO1, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
• 機能のキーワード: methyltransferase, rossmann-like fold, sam-dependent, transferase
• 由来する生物種: Micromonospora carbonacea
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28716.15

構造登録者

McCulloch, K.M.,Starbird, C.A.,Chen, Q.,Perry, N.A.,Berndt, S.,Yamakawa, I.,Loukachevitch, L.V.,Iverson, T.M. (登録日: 2016-08-25, 公開日: 2017-09-06, 最終更新日: 2023-10-04)

主引用文献

Starbird, C.A.,Perry, N.A.,Chen, Q.,Berndt, S.,Yamakawa, I.,Loukachevitch, L.V.,Limbrick, E.M.,Bachmann, B.O.,Iverson, T.M.,McCulloch, K.M.
The Structure of the Bifunctional Everninomicin Biosynthetic Enzyme EvdMO1 Suggests Independent Activity of the Fused Methyltransferase-Oxidase Domains.
Biochemistry, 57:6827-6837, 2018

PubMed Abstract: Members of the orthosomycin family of natural products are decorated polysaccharides with potent antibiotic activity and complex biosynthetic pathways. The defining feature of the orthosomycins is an orthoester linkage between carbohydrate moieties that is necessary for antibiotic activity and is likely formed by a family of conserved oxygenases. Everninomicins are octasaccharide orthosomycins produced by Micromonospora carbonacea that have two orthoester linkages and a methylenedioxy bridge, three features whose formation logically requires oxidative chemistry. Correspondingly, the evd gene cluster encoding everninomicin D encodes two monofunctional nonheme iron, α-ketoglutarate-dependent oxygenases and one bifunctional enzyme with an N-terminal methyltransferase domain and a C-terminal oxygenase domain. To investigate whether the activities of these domains are linked in the bifunctional enzyme EvdMO1, we determined the structure of the N-terminal methyltransferase domain to 1.1 Å and that of the full-length protein to 3.35 Å resolution. Both domains of EvdMO1 adopt the canonical folds of their respective superfamilies and are connected by a short linker. Each domain's active site is oriented such that it faces away from the other domain, and there is no evidence of a channel connecting the two. Our results support EvdMO1 working as a bifunctional enzyme with independent catalytic activities.

PubMed: 30525509
DOI: 10.1021/acs.biochem.8b00836

実験手法

X-RAY DIFFRACTION (1.1004 Å)