Linked Life Data

15632150

Source:http://linkedlifedata.com/resource/pubmed/id/15632150

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2005-2-28
pubmed:abstractText
Although many proteins require the binding of a ligand to be functional, the role of ligand binding during folding is scarcely investigated. Here, we have reported the influence of the flavin mononucleotide (FMN) cofactor on the global stability and folding kinetics of Azotobacter vinelandii holoflavodoxin. Earlier studies have revealed that A. vinelandii apoflavodoxin kinetically folds according to the four-state mechanism: I(1) <=> unfolded apoflavodoxin <=> I(2) <=> native apoflavodoxin. I(1)an off-pathway molten globule-like is intermediate that populates during denaturant-induced equilibrium unfolding; I(2) is a high energy on-pathway folding intermediate that never populates to a significant extent. Here, we have presented extensive denaturant-induced equilibrium unfolding data of holoflavodoxin, holoflavodoxin with excess FMN, and apoflavodoxin as well as kinetic folding and unfolding data of holoflavodoxin. All folding data are excellently described by a five-state mechanism: I(1) + FMN <=> unfolded apoflavodoxin + FMN <=> I(2) + FMN <=> native apoflavodoxin + FMN<=> holoflavodoxin. The last step in flavodoxin folding is thus the binding of FMN to native apoflavodoxin. I(1),I(2), and unfolded apoflavodoxin do not interact to a significantextent with FMN. The autonomous formation of native apoflavodoxin is essential during holoflavodoxin folding. Excess FMN does not accelerate holoflavodoxin folding, and FMN does not act as a nucleation site for folding. The stability of holoflavodoxin is so high that even under strongly denaturing conditions FMN needs to be released first before global unfolding of the protein can occur.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7836-44
pubmed:meshHeading
pubmed-meshheading:15632150-Azotobacter vinelandii, pubmed-meshheading:15632150-Circular Dichroism, pubmed-meshheading:15632150-Crystallography, X-Ray, pubmed-meshheading:15632150-Diphosphates, pubmed-meshheading:15632150-Dose-Response Relationship, Drug, pubmed-meshheading:15632150-Flavins, pubmed-meshheading:15632150-Flavodoxin, pubmed-meshheading:15632150-Guanidine, pubmed-meshheading:15632150-Kinetics, pubmed-meshheading:15632150-Ligands, pubmed-meshheading:15632150-Models, Chemical, pubmed-meshheading:15632150-Models, Molecular, pubmed-meshheading:15632150-Nucleotides, pubmed-meshheading:15632150-Peptides, pubmed-meshheading:15632150-Potassium, pubmed-meshheading:15632150-Protein Binding, pubmed-meshheading:15632150-Protein Folding, pubmed-meshheading:15632150-Recombinant Proteins, pubmed-meshheading:15632150-Spectrometry, Fluorescence, pubmed-meshheading:15632150-Thermodynamics, pubmed-meshheading:15632150-Time Factors
pubmed:year
2005
pubmed:articleTitle
Last in, first out: the role of cofactor binding in flavodoxin folding.
pubmed:affiliation
Department of Agrotechnology and Food Sciences, Laboratory of Biochemistry, Wageningen University, Dreijenlaan 3, NL-6703 HA Wageningen, The Netherlands.
pubmed:publicationType
Journal Article