7F39

The structure of flavin transferase FmnB

Summary for 7F39

• Entry DOI: 10.2210/pdb7f39/pdb
• Descriptor: FAD:protein FMN transferase (2 entities in total)
• Functional Keywords: fmn transferase, transferase
• Biological source: Listeria monocytogenes serotype 1/2a (strain 10403S)
• Total number of polymer chains: 1
• Total formula weight: 37713.43

Authors

Cheng, W.,Zheng, Y.H. (deposition date: 2021-06-15, release date: 2021-11-03, Last modification date: 2024-05-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.888 Å)