WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases.

Protein Sci.2007 Oct;16(10):2301-5

{{ author.authorName }}^{{{getOrganisationIndexOf(author)}}} {{ author.authorName }}^{{{getOrganisationIndexOf(author)}}}

+ et al

[No authors listed]

Author information

^{{index+1}} {{ organisation }}

摘要

The crystal structure of the flavodoxin-like protein WrbA with oxidized FMN bound reveals a close relationship to mammalian NAD(P)H:quinone oxidoreductase, Nqo1. Structural comparison of WrbA, flavodoxin, and Nqo1 indicates how the twisted open-sheet fold of flavodoxins is elaborated to form multimers that extend catalytic function from one-electron transfer between protein partners using FMN to two-electron reduction of xenobiotics using FAD. The structure suggests a novel physiological role for WrbA and Nqo1.

KEYWORDS: {{ getKeywords(articleDetailText.words) }}

基因功能

{{$index+1}}.{{ gene }}

图表

‹ › ×

原始数据

保存测序数据

Sample name	Organism	Experiment title	Sample type	Library instrument	Attributes
Sample name	Organism	Experiment title	Sample type	Library instrument	{{attr}}
{{ dataList.sampleTitle }}	{{ dataList.organism }}	{{ dataList.expermentTitle }}	{{ dataList.sampleType }}	{{ dataList.libraryInstrument }}	{{ showAttributeName(index,attr,dataList.attributes) }}

WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases.

摘要

基因功能

图表

基因

原始数据

文献解读

分析平台

分析平台

分析流程

{{currentAnalyse.title}}