2O1S

1-deoxy-D-xylulose 5-phosphate synthase (DXS) from Escherichia coli

2O1S の概要

• エントリーDOI: 10.2210/pdb2o1s/pdb
• 関連するPDBエントリー: 2O1X
• 分子名称: 1-deoxy-D-xylulose-5-phosphate synthase, MAGNESIUM ION, POTASSIUM ION, ... (6 entities in total)
• 機能のキーワード: dxs, thiamine, isoprenoid, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 276643.35

構造登録者

Xiang, S.,Usunow, G.,Lange, G.,Busch, M.,Tong, L. (登録日: 2006-11-29, 公開日: 2006-12-26, 最終更新日: 2024-11-13)

主引用文献

Xiang, S.,Usunow, G.,Lange, G.,Busch, M.,Tong, L.
Crystal Structure of 1-Deoxy-D-xylulose 5-Phosphate Synthase, a Crucial Enzyme for Isoprenoids Biosynthesis.
J.Biol.Chem., 282:2676-2682, 2007

PubMed Abstract: Isopentenyl pyrophosphate (IPP) is a common precursor for the synthesis of all isoprenoids, which have important functions in living organisms. IPP is produced by the mevalonate pathway in archaea, fungi, and animals. In contrast, IPP is synthesized by a mevalonate-independent pathway in most bacteria, algae, and plant plastids. 1-Deoxy-D-xylulose 5-phosphate synthase (DXS) catalyzes the first and the rate-limiting step of the mevalonate-independent pathway and is an attractive target for the development of novel antibiotics, antimalarials, and herbicides. We report here the first structural information on DXS, from Escherichia coli and Deinococcus radiodurans, in complex with the coenzyme thiamine pyrophosphate (TPP). The structure contains three domains (I, II, and III), each of which bears homology to the equivalent domains in transketolase and the E1 subunit of pyruvate dehydrogenase. However, DXS has a novel arrangement of these domains as compared with the other enzymes, such that the active site of DXS is located at the interface of domains I and II in the same monomer, whereas that of transketolase is located at the interface of the dimer. The coenzyme TPP is mostly buried in the complex, but the C-2 atom of its thiazolium ring is exposed to a pocket that is the substrate-binding site. The structures identify residues that may have important roles in catalysis, which have been confirmed by our mutagenesis studies.

PubMed: 17135236
DOI: 10.1074/jbc.M610235200

実験手法

X-RAY DIFFRACTION (2.4 Å)