7F39

The structure of flavin transferase FmnB

7F39 の概要

• エントリーDOI: 10.2210/pdb7f39/pdb
• 分子名称: FAD:protein FMN transferase (2 entities in total)
• 機能のキーワード: fmn transferase, transferase
• 由来する生物種: Listeria monocytogenes serotype 1/2a (strain 10403S)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37713.43

構造登録者

Cheng, W.,Zheng, Y.H. (登録日: 2021-06-15, 公開日: 2021-11-03, 最終更新日: 2024-05-29)

主引用文献

Zheng, Y.,Yan, W.,Dou, C.,Zhou, D.,Chen, Y.,Jin, Y.,Yang, L.,Zeng, X.,Cheng, W.
Structural insights into the catalytic and inhibitory mechanisms of the flavin transferase FmnB in Listeria monocytogenes.
MedComm (2020), 3:e99-e99, 2022

PubMed Abstract: , a food-borne Gram-positive pathogen, often causes diseases such as gastroenteritis, bacterial sepsis, and meningitis. Newly discovered extracellular electron transfer (EET) from plays critical roles in the generation of redox molecules as electron carriers in bacteria. A Mg-dependent protein flavin mononucleotide (FMN) transferase (FmnB; UniProt: LMRG_02181) in EET is responsible for the transfer of electrons from intracellular to extracellular by hydrolyzing cofactor flavin adenine dinucleotide (FAD) and transferring FMN. FmnB homologs have been investigated in Gram-negative bacteria but have been less well studied in Gram-positive bacteria. In particular, the catalytic and inhibitory mechanisms of FmnB homologs remain elusive. Here, we report a series of crystal structures of apo-FmnB and FmnB complexed with substrate FAD, three inhibitors AMP, ADP, and ATP, revealing the unusual catalytic triad center (Asp301-Ser257-His273) of FmnB. The three inhibitors indeed inhibited the activity of FmnB in varying degrees by occupying the binding site of the FAD substrate. The key residue Arg262 of FmnB was profoundly affected by ADP but not AMP or ATP. Overall, our studies not only provide insights into the promiscuous ligand recognition behavior of FmnB but also shed light on its catalytic and inhibitory mechanisms.

PubMed: 35281791
DOI: 10.1002/mco2.99

実験手法

X-RAY DIFFRACTION (1.888 Å)