3FEM

Structure of the synthase subunit Pdx1.1 (Snz1) of PLP synthase from Saccharomyces cerevisiae

3FEM の概要

• エントリーDOI: 10.2210/pdb3fem/pdb
• 関連するPDBエントリー: 1ZNN 2ISS 2NV1 2NV2
• 分子名称: Pyridoxine biosynthesis protein SNZ1 (2 entities in total)
• 機能のキーワード: (beta/alpha)8-barrel, synthase, pyridoxine biosynthesis, biosynthetic protein, transferase
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 191147.32

構造登録者

Strohmeier, M.,Windeisen, V.,Sinning, I.,Tews, I. (登録日: 2008-11-30, 公開日: 2009-06-16, 最終更新日: 2023-11-01)

主引用文献

Neuwirth, M.,Strohmeier, M.,Windeisen, V.,Wallner, S.,Deller, S.,Rippe, K.,Sinning, I.,Macheroux, P.,Tews, I.
X-ray crystal structure of Saccharomyces cerevisiae Pdx1 provides insights into the oligomeric nature of PLP synthases.
Febs Lett., 583:2179-2186, 2009

PubMed Abstract: The universal enzymatic cofactor vitamin B6 can be synthesized as pyridoxal 5-phosphate (PLP) by the glutamine amidotransferase Pdx1. We show that Saccharomyces cerevisiae Pdx1 is hexameric by analytical ultracentrifugation and by crystallographic 3D structure determination. Bacterial homologues were previously reported to exist in hexamer:dodecamer equilibrium. A small sequence insertion found in yeast Pdx1 elevates the dodecamer dissociation constant when introduced into Bacillus subtilis Pdx1. Further, we demonstrate that the yeast Pdx1 C-terminus contacts an adjacent subunit, and deletion of this segment decreases enzymatic activity 3.5-fold, suggesting a role in catalysis.

PubMed: 19523954
DOI: 10.1016/j.febslet.2009.06.009

実験手法

X-RAY DIFFRACTION (3.02 Å)