8HDF

Full length crystal structure of mycobacterium tuberculosis FadD23 in complex with ANP and PLM

8HDF の概要

• エントリーDOI: 10.2210/pdb8hdf/pdb
• 分子名称: Long-chain-fatty-acid--AMP ligase FadD23, PALMITIC ACID, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total)
• 機能のキーワード: long-chain-fatty-acid--amp ligase, biosynthetic protein
• 由来する生物種: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 65964.64

構造登録者

Yan, M.R.,Liu, X.,Zhang, W.,Rao, Z.H. (登録日: 2022-11-04, 公開日: 2023-02-15, 最終更新日: 2024-05-29)

主引用文献

Yan, M.,Cao, L.,Zhao, L.,Zhou, W.,Liu, X.,Zhang, W.,Rao, Z.
The Key Roles of Mycobacterium tuberculosis FadD23 C-terminal Domain in Catalytic Mechanisms.
Front Microbiol, 14:1090534-1090534, 2023

PubMed Abstract: Sulfolipid-1 (SL-1) is located in the () cell wall, and is essential for pathogen virulence and intracellular growth. Multiple proteins (e.g., Pks2, FadD23, PapA1, and MmpL8) in the SL-1 synthesis pathway can be treated as drug targets, but, to date, their structures have not been solved. The crystal structures of FadD23 bound to ATP or hexadecanoyl adenylate was determined in this study. We have also investigated long-chain saturated fatty acids as biological substrates of FadD23 through structural, biological, and chemical analyses. The mutation at the active site of FadD23 greatly influences enzymatic activity. Meanwhile, the FadD23 N-terminal domain alone cannot bind palmitic acid without C-terminal domain facilitation since it is almost inactive after removing the C-terminal domain. FadD23 is the first protein in the SL-1 synthesis pathway whose structure has been solved. These results reveal the importance of the C-terminal domain in the catalytic mechanism.

PubMed: 36896429
DOI: 10.3389/fmicb.2023.1090534

実験手法

X-RAY DIFFRACTION (2.24 Å)