1ITZ

Maize Transketolase in complex with TPP

1ITZ の概要

• エントリーDOI: 10.2210/pdb1itz/pdb
• 分子名称: Transketolase, MAGNESIUM ION, THIAMINE DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: calvin cycle, transketolase, zea mays, cofactor, thiamine pyrophosphate, plant, transferase
• 由来する生物種: Zea mays
• 細胞内の位置: Plastid, chloroplast thylakoid membrane (By similarity): Q7SIC9
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 220574.54

構造登録者

Gerhardt, S.,Echt, S.,Bader, G.,Freigang, J.,Busch, M.,Bacher, A.,Huber, R.,Fischer, M. (登録日: 2002-02-15, 公開日: 2003-02-15, 最終更新日: 2023-12-27)

主引用文献

Gerhardt, S.,Echt, S.,Busch, M.,Freigang, J.,Auerbach, G.,Bader, G.,Martin, W.F.,Bacher, A.,Huber, R.,Fischer, M.
Structure and properties of an engineered transketolase from maize
PLANT PHYSIOL., 132:1941-1949, 2003

PubMed Abstract: The gene specifying plastid transketolase (TK) of maize (Zea mays) was cloned from a cDNA library by southern blotting using a heterologous probe from sorghum (Sorghum bicolor). A recombinant fusion protein comprising thioredoxin of Escherichia coli and mature TK of maize was expressed at a high level in E. coli and cleaved with thrombin, affording plastid TK. The protein in complex with thiamine pyrophoshate was crystallized, and its structure was solved by molecular replacement. The enzyme is a C2 symmetric homodimer closely similar to the enzyme from yeast (Saccharomyces cerevisiae). Each subunit is folded into three domains. The two topologically equivalent active sites are located in the subunit interface region and resemble those of the yeast enzyme.

PubMed: 12913150
DOI: 10.1104/pp.103.020982

実験手法

X-RAY DIFFRACTION (2.3 Å)