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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2008-2-1
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pubmed:abstractText |
The key three-dimensional features of flavohemoglobins have been unveiled by X-ray crystallographic investigations carried out on the Alcaligenes eutrophus and Escherichia coli proteins. Flavohemoglobins are made of a globin domain fused with a ferredoxin reductase-like FAD binding module and display highly conserved sequences in the active sites of both the heme-binding domain and the flavin-binding domain. Structural studies are discussed and methodological approaches to the solution of the crystal structures and to the analysis of the relevant stereochemical properties of the active sites are presented. The understanding of the structural properties of flavohemoglobins serves as a guide for testing biological hypotheses and allows for a rational evaluation of structure-based alignments within the flavohemoglobin family.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Dihydropteridine Reductase,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Flavin-Adenine Dinucleotide,
http://linkedlifedata.com/resource/pubmed/chemical/Heme,
http://linkedlifedata.com/resource/pubmed/chemical/Hemeproteins,
http://linkedlifedata.com/resource/pubmed/chemical/NAD,
http://linkedlifedata.com/resource/pubmed/chemical/NADH, NADPH Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/flavohemoprotein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/hmp protein, E coli
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pubmed:status |
MEDLINE
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pubmed:issn |
0076-6879
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
436
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
187-202
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pubmed:meshHeading |
pubmed-meshheading:18237633-Amino Acid Sequence,
pubmed-meshheading:18237633-Bacterial Proteins,
pubmed-meshheading:18237633-Binding Sites,
pubmed-meshheading:18237633-Crystallography, X-Ray,
pubmed-meshheading:18237633-Cupriavidus necator,
pubmed-meshheading:18237633-Dihydropteridine Reductase,
pubmed-meshheading:18237633-Escherichia coli,
pubmed-meshheading:18237633-Escherichia coli Proteins,
pubmed-meshheading:18237633-Flavin-Adenine Dinucleotide,
pubmed-meshheading:18237633-Heme,
pubmed-meshheading:18237633-Hemeproteins,
pubmed-meshheading:18237633-Models, Molecular,
pubmed-meshheading:18237633-Molecular Sequence Data,
pubmed-meshheading:18237633-NAD,
pubmed-meshheading:18237633-NADH, NADPH Oxidoreductases,
pubmed-meshheading:18237633-Phospholipids,
pubmed-meshheading:18237633-Protein Folding,
pubmed-meshheading:18237633-Protein Structure, Tertiary,
pubmed-meshheading:18237633-Sequence Homology, Amino Acid,
pubmed-meshheading:18237633-Species Specificity
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pubmed:year |
2008
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pubmed:articleTitle |
Structural studies on flavohemoglobins.
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pubmed:affiliation |
CNR Institute of Molecular Biology and Pathology, University of Rome La Sapienza, Rome, Italy.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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