Structural basis for the thioredoxin-like activity profile of the glutaredoxin-like NrdH-redoxin from Escherichia coli
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Structural basis of cellular redox regulation by human TRP14NrdH-redoxin of Mycobacterium tuberculosis and Corynebacterium glutamicum Dimerizes at High Protein Concentration and Exclusively Receives Electrons from Thioredoxin ReductaseTuning of thioredoxin redox properties by intramolecular hydrogen bondsMycoredoxin-1 is one of the missing links in the oxidative stress defence mechanism of MycobacteriaLow stability of the reduced state of Mycobacterium tuberculosis NrdH redoxin.RNRdb, a curated database of the universal enzyme family ribonucleotide reductase, reveals a high level of misannotation in sequences deposited to Genbank.Staphylococcus aureus NrdH redoxin is a reductant of the class Ib ribonucleotide reductaseA bioinformatic analysis of ribonucleotide reductase genes in phage genomes and metagenomes.Class I ribonucleotide reductases: metallocofactor assembly and repair in vitro and in vivo.An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations.NrdH Redoxin enhances resistance to multiple oxidative stresses by acting as a peroxidase cofactor in Corynebacterium glutamicumTranscriptional responses of Escherichia coli K-12 and O157:H7 associated with lettuce leaves.The concerted action of a positive charge and hydrogen bonds dynamically regulates the pKa of the nucleophilic cysteine in the NrdH-redoxin family.S434F in NrdE generates the thermosensitive phenotype of corynebacterium ammoniagenes CH31 and enhances thermolability by increasing the surface hydrophobicity of the NrdE(Ts) protein.Oxygen- and NssR-dependent globin expression and enhanced iron acquisition in the response of campylobacter to nitrosative stressMycobacteriophage L5Gp56, a novel member of the NrdH family of redoxins.Cooperative and allosterically controlled nucleotide binding regulates the DNA binding activity of NrdR.Ferredoxin:thioredoxin reductase (FTR) links the regulation of oxygenic photosynthesis to deeply rooted bacteria.An essential thioredoxin is involved in the control of the cell cycle in the bacterium Caulobacter crescentus.The specificity of thioredoxins and glutaredoxins is determined by electrostatic and geometric complementarity.
P2860
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P2860
Structural basis for the thioredoxin-like activity profile of the glutaredoxin-like NrdH-redoxin from Escherichia coli
description
2001 nî lūn-bûn
@nan
2001 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Structural basis for the thior ...... -redoxin from Escherichia coli
@ast
Structural basis for the thior ...... -redoxin from Escherichia coli
@en
Structural basis for the thior ...... -redoxin from Escherichia coli
@nl
type
label
Structural basis for the thior ...... -redoxin from Escherichia coli
@ast
Structural basis for the thior ...... -redoxin from Escherichia coli
@en
Structural basis for the thior ...... -redoxin from Escherichia coli
@nl
prefLabel
Structural basis for the thior ...... -redoxin from Escherichia coli
@ast
Structural basis for the thior ...... -redoxin from Escherichia coli
@en
Structural basis for the thior ...... -redoxin from Escherichia coli
@nl
P2860
P50
P356
P1476
Structural basis for the thior ...... -redoxin from Escherichia coli
@en
P2093
P2860
P304
P356
10.1074/JBC.M105094200
P407
P577
2001-09-21T00:00:00Z