2G1H

Structure of E.coli FabD complexed with glycerol

2G1H の概要

• エントリーDOI: 10.2210/pdb2g1h/pdb
• 分子名称: Malonyl CoA-acyl carrier protein transacylase, GLYCEROL (3 entities in total)
• 機能のキーワード: complex, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32403.98

構造登録者

Oefner, C. (登録日: 2006-02-14, 公開日: 2006-05-30, 最終更新日: 2023-10-25)

主引用文献

Oefner, C.,Schulz, H.,D'Arcy, A.,Dale, G.E.
Mapping the active site of Escherichia coli malonyl-CoA-acyl carrier protein transacylase (FabD) by protein crystallography.
Acta Crystallogr.,Sect.D, 62:613-618, 2006

PubMed Abstract: Malonyl-CoA-acyl carrier protein transacylase (FabD; EC 2.3.1.39) is a key enzyme in the fatty-acid biosynthesis pathway of bacteria, catalyzing the transfer of a malonyl moiety from malonyl-CoA to holo acyl carrier protein (ACP), generating malonyl-ACP and free CoASH. Malonyl-ACP, which is the product of this reaction, is the key building block for de novo fatty-acid biosynthesis. Various binary complex structures of the Escherichia coli enzyme are presented, including that of the natural substrate malonyl-CoA, indicating the functional role of the highly conserved amino acids Gln11, Ser92, Arg117 and His201 and the stabilizing function of the preformed oxyanion hole during the enzymatic reaction. Based on the presented structural data, a possible new catalytic enzyme mechanism is discussed. The data obtained could be used in aiding the process of rational inhibitor design.

PubMed: 16699188
DOI: 10.1107/S0907444906009474

実験手法

X-RAY DIFFRACTION (1.86 Å)