5D6N

Crystal structure of a mycobacterial protein

5D6N の概要

• エントリーDOI: 10.2210/pdb5d6n/pdb
• 関連するPDBエントリー: 5D6J
• 分子名称: Acyl-CoA synthase (2 entities in total)
• 機能のキーワード: mycobacterium smegmatis, ligase
• 由来する生物種: Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 55442.92

構造登録者

Li, W.J.,Bi, L.J. (登録日: 2015-08-12, 公開日: 2016-03-02, 最終更新日: 2023-11-08)

主引用文献

Li, W.,Gu, S.,Fleming, J.,Bi, L.
Crystal structure of FadD32, an enzyme essential for mycolic acid biosynthesis in mycobacteria.
Sci Rep, 5:15493-15493, 2015

PubMed Abstract: Fatty acid degradation protein D32 (FadD32), an enzyme required for mycolic acid biosynthesis and essential for mycobacterial growth, has recently been identified as a valid and promising target for anti-tuberculosis drug development. Here we report the crystal structures of Mycobacterium smegmatis FadD32 in the apo and ATP-bound states at 2.4 Å and 2.25 Å resolution, respectively. FadD32 consists of two globular domains connected by a flexible linker. ATP binds in a cleft at the interface between the N- and C-terminal domains and its binding induces significant local conformational changes in FadD32. The binding sites of meromycolic acid and phosphopantetheine are identified by structural comparison with other members of the adenylating enzyme superfamily. These results will improve our understanding of the catalytic mechanism of FadD32 and help in the design of inhibitors of this essential enzyme.

PubMed: 26628098
DOI: 10.1038/srep15493

実験手法

X-RAY DIFFRACTION (2.401 Å)