Conformational Dynamics of Escherichia coliFlavodoxins in Apo- and Holo-States by Solution NMR Spectroscopy
- 影响因子：
0.0
- 发表刊物：
PLoS One
- 摘要：
Flavodoxins are a family of small FMN-binding proteins that commonly exist in prokaryotes. They utilize a non-covalently bound FMN molecule to act as the redox center during the electron transfer processes in various important biological pathways. Although extensive investigations were performed, detailed molecular mechanisms of cofactor binding and electron transfer remain elusive. Herein we report the solution NMR studies on Escherichia coli flavodoxins FldA and YqcA, belonging to the long-chain and short-chain flavodoxin subfamilies respectively. Our structural studies demonstrate that both proteins show the typical flavodoxin fold, with extensive conformational exchanges observed near the FMN binding pocket in their apo-forms. Cofactor binding significantly stabilizes both proteins as revealed by the extension of secondary structures in the holo-forms, and the overall rigidity shown by the backbone dynamics data. However, the 50 s loops of both proteins in the holo-form still show conformational exchanges on the µs-ms timescales, which appears to be a common feature in the flavodoxin family, and might play an important role in structural fine-tuning during the electron transfer reactions.
- 论文类型：
期刊论文
- 论文编号：
46
- 卷号：
9
- 期号：
8
- 页面范围：
e103936
- 是否译文：
否
- 发表时间：
2014-08-05
- 收录刊物：
SCI
- 发布期刊链接：
- 第一作者：
Ye Qian
- 通讯作者：
Jin Changwen
- 全部作者：
Hu Yunfei
