Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2018 Feb 15;9:231. doi: 10.3389/fmicb.2018.00231

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright © 2018 Su, Su, Liu, Zhang, He, Huang, Xu and Gu.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

PMC Copyright notice

Structure of BdsA-FMN complex. (A) The electron density map (contoured at 2.0σ) reveals the existence of FMN within BdsA active pocket. (B) The pocket constituting of IS1, IS2, IS3, and IS5 forms the active site of FMN and substrate binding. (C) Structure comparison of the apo and FMN bound BdsA. Yellow ribbon represents the apo-BdsA structure and cyan ribbon stands for the FMN bound structure. The FMN is depicted in color sticks. Distinct structural rearrangements occur at residues Phe56, Val137, and Phe246. (D) The docking result of the BdsA-FMN-DBT sulfone complex. Residues constituting the binding pocket are shown as green sticks. The cofactor FMN is shown as gray sticks. DBT sulfone is shown as cyan sticks. V137, S139, H156, R159, Y160, and L230 play significant roles in FMN binding. F12, F56, F246, V248, H316, and V372 play directional roles in substrate binding.