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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2002-8-28
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pubmed:abstractText |
The X-ray crystal structure of the apo-form of the Fur protein from Rhizobium leguminosarum has been solved at 2.7 A resolution. Small-angle X-ray scattering was used to give information on the solution conformation of the protein. The Fur homodimer folds into two domains. The N-terminal domain is formed from the packing of two helix-turn-helix motifs while the C-terminal domain appears primarily to stabilize the dimeric state of the protein.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0300-5127
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
771-4
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pubmed:dateRevised |
2010-10-19
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pubmed:meshHeading |
pubmed-meshheading:12196192-Amino Acid Sequence,
pubmed-meshheading:12196192-Bacterial Proteins,
pubmed-meshheading:12196192-Binding Sites,
pubmed-meshheading:12196192-Crystallography, X-Ray,
pubmed-meshheading:12196192-Iron,
pubmed-meshheading:12196192-Metalloproteins,
pubmed-meshheading:12196192-Models, Molecular,
pubmed-meshheading:12196192-Protein Conformation,
pubmed-meshheading:12196192-Repressor Proteins,
pubmed-meshheading:12196192-Rhizobium leguminosarum
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pubmed:year |
2002
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pubmed:articleTitle |
Structural studies of the Fur protein from Rhizobium leguminosarum.
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pubmed:affiliation |
School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK.
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pubmed:publicationType |
Journal Article
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