Source:http://linkedlifedata.com/resource/pubmed/id/11872744
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
19
|
| pubmed:dateCreated |
2002-5-6
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| pubmed:abstractText |
Maize ferredoxin-NADP(+) reductase (FNR) consists of flavin adenine dinucleotide (FAD) and NADP(+) binding domains with a FAD molecule bound noncovalently in the cleft between these domains. The structural changes of FNR induced by dissociation of FAD have been characterized by a combination of optical and biochemical methods. The CD spectrum of the FAD-depleted FNR (apo-FNR) suggested that removal of FAD from holo-FNR produced an intermediate conformational state with partially disrupted secondary and tertiary structures. Small angle x-ray scattering indicated that apo-FNR assumes a conformation that is less globular in comparison with holo-FNR but is not completely chain-like. Interestingly, the replacement of tyrosine 95 responsible for FAD binding with alanine resulted in a molecular form similar to apo-protein of the wild-type enzyme. Both apo- and Y95A-FNR species bound to Cibacron Blue affinity resin, indicating the presence of a native-like conformation for the NADP(+) binding domain. On the other hand, no evidence was found for the existence of folded conformations in the FAD binding domains of these proteins. These results suggested that FAD-depleted FNR assumes a partially folded structure with a residual NADP(+) binding domain but a disordered FAD binding domain.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alanine,
http://linkedlifedata.com/resource/pubmed/chemical/Cibacron Blue F 3GA,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Ferredoxin-NADP Reductase,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Synthesis Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Triazines
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| pubmed:status |
MEDLINE
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| pubmed:month |
May
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
10
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| pubmed:volume |
277
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
17101-7
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11872744-Alanine,
pubmed-meshheading:11872744-Circular Dichroism,
pubmed-meshheading:11872744-Crystallography, X-Ray,
pubmed-meshheading:11872744-Dose-Response Relationship, Drug,
pubmed-meshheading:11872744-Enzyme Inhibitors,
pubmed-meshheading:11872744-Ferredoxin-NADP Reductase,
pubmed-meshheading:11872744-Hydrogen-Ion Concentration,
pubmed-meshheading:11872744-Models, Chemical,
pubmed-meshheading:11872744-Models, Molecular,
pubmed-meshheading:11872744-Protein Binding,
pubmed-meshheading:11872744-Protein Conformation,
pubmed-meshheading:11872744-Protein Folding,
pubmed-meshheading:11872744-Protein Structure, Secondary,
pubmed-meshheading:11872744-Protein Structure, Tertiary,
pubmed-meshheading:11872744-Protein Synthesis Inhibitors,
pubmed-meshheading:11872744-Scattering, Radiation,
pubmed-meshheading:11872744-Spectrometry, Fluorescence,
pubmed-meshheading:11872744-Thermodynamics,
pubmed-meshheading:11872744-Time Factors,
pubmed-meshheading:11872744-Triazines,
pubmed-meshheading:11872744-Zea mays
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| pubmed:year |
2002
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| pubmed:articleTitle |
Partially folded structure of flavin adenine dinucleotide-depleted ferredoxin-NADP+ reductase with residual NADP+ binding domain.
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| pubmed:affiliation |
Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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