Source:http://linkedlifedata.com/resource/pubmed/id/17431550
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2007-5-16
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pubmed:abstractText |
NifU-like proteins are a highly conserved protein that serves as the scaffold for assembly of Fe-S clusters. Chloroplastic NifU-like proteins have tandem NifU like domains, named domain I and domain II. Although the amino acid sequences of these domains are very similar to each other, the predicted functional region for the Fe-S cluster assembly, the CXXC motif, exists only in domain I. The structure of the domain II of chloroplastic NifU-like protein OsNifU1A has an alpha-beta sandwich structure containing two alpha helices located on one side of the beta-sheet. The electrostatic surface potential of OsNifU1A domain II is predominantly positively charged. Chloroplastic NifU-like proteins are targeted to ferredoxin for transferring the Fe-S cluster. The ferredoxin presents an overall negatively charged surface, which may evoke an electrostatic association with OsNifU1A domain II.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0925-2738
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
38
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
161-4
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:17431550-Chloroplasts,
pubmed-meshheading:17431550-Models, Molecular,
pubmed-meshheading:17431550-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:17431550-Oryza sativa,
pubmed-meshheading:17431550-Plant Proteins,
pubmed-meshheading:17431550-Protein Structure, Secondary,
pubmed-meshheading:17431550-Protein Structure, Tertiary,
pubmed-meshheading:17431550-Static Electricity
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pubmed:year |
2007
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pubmed:articleTitle |
The NMR structure of the domain II of a chloroplastic NifU-like protein OsNifU1A.
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pubmed:affiliation |
Laboratory of Structural Biology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo, Hokkaido, 060-0812, Japan.
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pubmed:publicationType |
Journal Article
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