5GWW

Structure of MoeN5-Sso7d fusion protein in complex with a permethylated substrate analogue

5GWW の概要

• エントリーDOI: 10.2210/pdb5gww/pdb
• 関連するPDBエントリー: 5B02 5GWV 6J8V 6J8W
• 分子名称: MoeN5,DNA-binding protein 7d, methyl (2R)-3-dimethoxyphosphoryloxy-2-[(2Z,6E)-3,7,11-trimethyldodeca-2,6,10-trienoxy]propanoate (3 entities in total)
• 機能のキーワード: moenomycin, antibiotics, biosynthesis, prenyl transferase, alpha helical, transferase, dna binding protein
• 由来する生物種: Streptomyces ghanaensis; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 150759.61

構造登録者

Ko, T.-P.,Guo, R.-T.,Chen, C.-C. (登録日: 2016-09-14, 公開日: 2017-09-20, 最終更新日: 2023-11-08)

主引用文献

Zhang, L.,Ko, T.-P.,Malwal, S.R.,Liu, W.,Zhou, S.,Yu, X.,Oldfield, E.,Guo, R.-T.,Chen, C.-C.
Complex structures of MoeN5 with substrate analogues suggest sequential catalytic mechanism.
Biochem. Biophys. Res. Commun., 511:800-805, 2019

PubMed Abstract: The antibiotic moenomycin A is a phosphoglycerate derivative with a C-moenocinyl chain and a branched oligosaccharide. Formation of the C-chain is catalyzed by the enzyme MoeN5 with geranyl pyrophosphate (GPP) and the sugar-linked 2-Z,E-farnesyl-3-phosphoglycerate (FPG) as its substrates. Previous complex crystal structures with GPP and long-chain alkyl glycosides suggested that GPP binds to the S1 site in a similar way as in most other α-helical prenyltransferases (PTs), and FPG is likely to assume a bent conformation in the S2 site. However, two FPG derivatives synthesized in the current study were found in the S1 site rather than S2 in their complex crystal structures with MoeN5. Apparently S1 is the preferred site for prenyl-containing ligand, and S2 binding may proceed only after S1 is occupied. Thus, like most trans-type PTs, MoeN5 may employ a sequential ionization-condensation-elimination mechanism that involves a carbocation intermediate.

PubMed: 30837154
DOI: 10.1016/j.bbrc.2019.02.131

実験手法

X-RAY DIFFRACTION (2.3 Å)