1DD8

CRYSTAL STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE I FROM ESCHERICHIA COLI

1DD8 の概要

• エントリーDOI: 10.2210/pdb1dd8/pdb
• 分子名称: BETA-KETOACYL [ACYL CARRIER PROTEIN] SYNTHASE I (2 entities in total)
• 機能のキーワード: thiolase fold, transferase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P0A953
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 170737.02

構造登録者

Olsen, J.G.,Kadziola, A.,von Wettstein-Knowles, P.,Siggaard-Andersen, M.,Lindquist, Y.,Larsen, S. (登録日: 1999-11-09, 公開日: 1999-11-18, 最終更新日: 2024-02-07)

主引用文献

Olsen, J.G.,Kadziola, A.,von Wettstein-Knowles, P.,Siggaard-Andersen, M.,Lindquist, Y.,Larsen, S.
The X-ray crystal structure of beta-ketoacyl [acyl carrier protein] synthase I.
FEBS Lett., 460:46-52, 1999

PubMed Abstract: The crystal structure of the fatty acid elongating enzyme beta-ketoacyl [acyl carrier protein] synthase I (KAS I) from Escherichia coli has been determined to 2.3 A resolution by molecular replacement using the recently solved crystal structure of KAS II as a search model. The crystal contains two independent dimers in the asymmetric unit. KAS I assumes the thiolase alpha(beta)alpha(beta)alpha fold. Electrostatic potential distribution reveals an acyl carrier protein docking site and a presumed substrate binding pocket was detected extending the active site. Both subunits contribute to each substrate binding site in the dimer.

PubMed: 10571059
DOI: 10.1016/S0014-5793(99)01303-4

実験手法

X-RAY DIFFRACTION (2.3 Å)