Source:http://linkedlifedata.com/resource/pubmed/id/16905545
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
42
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pubmed:dateCreated |
2006-10-16
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pubmed:databankReference | |
pubmed:abstractText |
Murine p22HBP, a 22-kDa monomer originally identified as a cytosolic heme-binding protein ubiquitously expressed in various tissues, has 27% sequence identity to murine SOUL, a heme-binding hexamer specifically expressed in the retina. In contrast to murine SOUL, which binds one heme per subunit via coordination of the Fe(III)-heme to a histidine, murine p22HBP binds one heme molecule per subunit with no specific axial ligand coordination of the Fe(III)-heme. Using intrinsic protein fluorescence quenching, the values for the dissociation constants of p22HBP for hemin and protoporphyrin-IX were determined to be in the low nanomolar range. The three-dimensional structure of murine p22HBP, the first for a protein from the SOUL/HBP family, was determined by NMR methods to consist of a 9-stranded distorted beta-barrel flanked by two long alpha-helices. Although homologous domains have been found in three bacterial proteins, two of which are transcription factors, the fold determined for p22HBP corresponds to a novel alpha plus beta fold in a eukaryotic protein. Chemical shift mapping localized the tetrapyrrole binding site to a hydrophobic cleft formed by residues from helix alphaA and an extended loop. In an attempt to assess the structural basis for tetrapyrrole binding in the SOUL/HBP family, models for the p22HBP-protoporphyrin-IX complex and the SOUL protein were generated by manual docking and automated methods.
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pubmed:grant | |
pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hebp1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Heme,
http://linkedlifedata.com/resource/pubmed/chemical/Hemeproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hemin,
http://linkedlifedata.com/resource/pubmed/chemical/Protoporphyrins,
http://linkedlifedata.com/resource/pubmed/chemical/Tetrapyrroles,
http://linkedlifedata.com/resource/pubmed/chemical/heme-binding protein,
http://linkedlifedata.com/resource/pubmed/chemical/protoporphyrin IX
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
281
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
31553-61
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16905545-Amino Acid Sequence,
pubmed-meshheading:16905545-Animals,
pubmed-meshheading:16905545-Carrier Proteins,
pubmed-meshheading:16905545-Heme,
pubmed-meshheading:16905545-Hemeproteins,
pubmed-meshheading:16905545-Hemin,
pubmed-meshheading:16905545-Humans,
pubmed-meshheading:16905545-Mice,
pubmed-meshheading:16905545-Molecular Sequence Data,
pubmed-meshheading:16905545-Protein Structure, Secondary,
pubmed-meshheading:16905545-Protoporphyrins,
pubmed-meshheading:16905545-Sequence Homology, Amino Acid,
pubmed-meshheading:16905545-Tetrapyrroles
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pubmed:year |
2006
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pubmed:articleTitle |
The first structure from the SOUL/HBP family of heme-binding proteins, murine P22HBP.
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pubmed:affiliation |
Rede de Química e Tecnologia, Centro de Química Fina e Biotecnologia, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516 Caparica, Portugal.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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