5HOQ

Apo structure of CalS11, TDP-rhamnose 3'-o-methyltransferase, an enzyme in Calicheamicin biosynthesis

「4PWR」から置き換えられました

5HOQ の概要

• エントリーDOI: 10.2210/pdb5hoq/pdb
• 分子名称: TDP-rhamnose 3'-O-methyltransferase (CalS11), SULFATE ION (3 entities in total)
• 機能のキーワード: rhamnose methyltransferase calicheamicin biosynthesis, transferase
• 由来する生物種: Micromonospora echinospora
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 145234.54

構造登録者

Han, L.,Helmich, K.E.,Singh, S.,Thorson, J.S.,Bingman, C.A.,Phillips Jr., G.N.,Enzyme Discovery for Natural Product Biosynthesis (NatPro) (登録日: 2016-01-19, 公開日: 2016-03-30, 最終更新日: 2025-10-22)

主引用文献

Han, L.,Singh, S.,Thorson, J.S.,Phillips, G.N.
Loop dynamics of thymidine diphosphate-rhamnose 3'-O-methyltransferase (CalS11), an enzyme in calicheamicin biosynthesis.
Struct Dyn., 3:012004-012004, 2016

PubMed Abstract: Structure analysis and ensemble refinement of the apo-structure of thymidine diphosphate (TDP)-rhamnose 3'-O-methyltransferase reveal a gate for substrate entry and product release. TDP-rhamnose 3'-O-methyltransferase (CalS11) catalyses a 3'-O-methylation of TDP-rhamnose, an intermediate in the biosynthesis of enediyne antitumor antibiotic calicheamicin. CalS11 operates at the sugar nucleotide stage prior to glycosylation step. Here, we present the crystal structure of the apo form of CalS11 at 1.89 Å resolution. We propose that the L2 loop functions as a gate facilitating and/or providing specificity for substrate entry or promoting product release. Ensemble refinement analysis slightly improves the crystallographic refinement statistics and furthermore provides a compelling way to visualize the dynamic model of loop L2, supporting the understanding of its proposed role in catalysis.

PubMed: 26958582
DOI: 10.1063/1.4941368

実験手法

X-RAY DIFFRACTION (1.793 Å)