2VNE

The X-ray structure of Norcoclaurine synthase from Thalictrum flavum

2VNE の概要

• エントリーDOI: 10.2210/pdb2vne/pdb
• 関連するPDBエントリー: 2VQ5
• 分子名称: S-NORCOCLAURINE SYNTHASE (2 entities in total)
• 機能のキーワード: lyase, norcoclaurine synthase, biosynthesis of benzylisoquinoline alkaloids
• 由来する生物種: THALICTRUM FLAVUM
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 45212.42

構造登録者

Ilari, A.,Franceschini, S.,Boffi, A.,Bonamore, A.,Pasquo, A. (登録日: 2008-02-04, 公開日: 2008-08-05, 最終更新日: 2024-10-23)

主引用文献

Ilari, A.,Franceschini, S.,Bonamore, A.,Arenghi, F.,Botta, B.,Macone, A.,Pasquo, A.,Bellucci, L.,Boffi, A.
Structural Basis of Enzymatic S-Norcoclaurine Biosynthesis.
J.Biol.Chem., 284:897-, 2009

PubMed Abstract: The enzyme norcoclaurine synthase (NCS) catalyzes the stereospecific Pictet-Spengler cyclization between dopamine and 4-hydroxyphenylacetaldehyde, the key step in the benzylisoquinoline alkaloid biosynthetic pathway. The crystallographic structure of norcoclaurine synthase from Thalictrum flavum in its complex with dopamine substrate and the nonreactive substrate analogue 4-hydroxybenzaldehyde has been solved at 2.1A resolution. NCS shares no common features with the functionally correlated "Pictet-Spenglerases" that catalyze the first step of the indole alkaloids pathways and conforms to the overall fold of the Bet v1-like protein. The active site of NCS is located within a 20-A-long catalytic tunnel and is shaped by the side chains of a tyrosine, a lysine, an aspartic, and a glutamic acid. The geometry of the amino acid side chains with respect to the substrates reveals the structural determinants that govern the mechanism of the stereoselective Pictet-Spengler cyclization, thus establishing an excellent foundation for the understanding of the finer details of the catalytic process. Site-directed mutations of the relevant residues confirm the assignment based on crystallographic findings.

PubMed: 19004827
DOI: 10.1074/JBC.M803738200

実験手法

X-RAY DIFFRACTION (2.72 Å)