1HND

CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III-COA COMPLEX

1HND の概要

• エントリーDOI: 10.2210/pdb1hnd/pdb
• 関連するPDBエントリー: 1hn9 1hnh 1hnj 1hnk
• 分子名称: BETA-KETOACYL-ACYL CARRIER PROTEIN SYNTHASE III, COENZYME A (3 entities in total)
• 機能のキーワード: fabh, transferase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P0A6R0
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34314.56

構造登録者

Qiu, X.,Janson, C.A.,Smith, W.W.,Head, M.,Lonsdale, J.,Konstantinidis, A.K. (登録日: 2000-12-07, 公開日: 2000-12-27, 最終更新日: 2024-04-03)

主引用文献

Qiu, X.,Janson, C.A.,Smith, W.W.,Head, M.,Lonsdale, J.,Konstantinidis, A.K.
Refined structures of beta-ketoacyl-acyl carrier protein synthase III.
J.Mol.Biol., 307:341-356, 2001

PubMed Abstract: beta-Ketoacyl-acyl carrier protein synthase III (FabH) is a condensing enzyme that plays central roles in fatty acid biosynthesis. Three-dimensional structures of E. coli FabH in the presence and absence of ligands have been refined to 1.46 A resolution. The structures of improved accuracy revealed detailed interactions involved in ligand binding. These structures also provided new insights into the FabH mechanism, e.g. the possible role of a water or hydroxyl anion in Cys112 deprotonation. A structure of the apo enzyme uncovered large conformational changes in the active site, exemplified by the disordering of four essential loops (84-86, 146-152, 185-217 and 305-307) and the movement of catalytic residues (Cys112 and His244). The disordering of the loops leads to greater than 50 % reduction in the FabH dimer interface, suggesting a dynamic nature for an unusually large portion of the dimer interface. The existence of a large solvent-accessible channel in the dimer interface as well as two cis-peptides (cis-Pro88 and cis-Phe308) in two of the disordered loops may explain the observed structural instabilities.

PubMed: 11243824
DOI: 10.1006/jmbi.2000.4457

実験手法

X-RAY DIFFRACTION (1.6 Å)