4EOU

Crystal structure of E. coli dihydrodipicolinate synthase with pyruvate and succinic semi-aldehyde bound in active site

「3UBS」から置き換えられました

4EOU の概要

• エントリーDOI: 10.2210/pdb4eou/pdb
• 関連するPDBエントリー: 1DHP 1YXC 3DU0
• 分子名称: Dihydrodipicolinate synthase, POTASSIUM ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: alpha/beta barrel, tim barrel, amino-acid biosynthesis, schiff base, lyase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P0A6L2
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 63292.70

構造登録者

Boughton, B.A.,Dobson, R.C.J.,Hutton, C.A. (登録日: 2012-04-15, 公開日: 2012-04-25, 最終更新日: 2024-11-06)

主引用文献

Boughton, B.A.,Dobson, R.C.,Hutton, C.A.
The crystal structure of dihydrodipicolinate synthase from Escherichia coli with bound pyruvate and succinic acid semialdehyde: Unambiguous resolution of the stereochemistry of the condensation product.
Proteins, 80:2117-2122, 2012

PubMed Abstract: The crystal structure of Escherichia coli dihydrodipicolinate synthase with pyruvate and substrate analogue succinic acid semialdehyde condensed with the active site lysine-161 was solved to a resolution of 2.3 Å. Comparative analysis to a previously reported structure both resolves the configuration at the aldol addition center, where the final addition product clearly displays the (S)-configuration, and the final conformation of the adduct within the active site. Direct comparison to two other crystal structures found in the Protein Data Bank, 1YXC, and 3DU0, demonstrates significant similarity between the active site residues of these structures.

PubMed: 22552955
DOI: 10.1002/prot.24106

実験手法

X-RAY DIFFRACTION (2.3 Å)