A Novel Haem-binding Interface in the 22 kDa Haem-binding Protein p22HBP
| Autor: | David A. Gell, Joel P. Mackay, Belinda J. Westman, John J. Welch, ChuKong Liew, Mitchell J. Weiss, Daniel Gorman |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Hemeproteins
Models Molecular Porphyrins Recombinant Fusion Proteins Molecular Sequence Data Heme Ligand Binding Protein Haem binding Biology Protein Structure Secondary Heme-Binding Proteins Protein structure Bacterial Proteins Structural Biology Animals Molecule Amino Acid Sequence Nuclear Magnetic Resonance Biomolecular Molecular Biology Binding Sites Circular Dichroism Affinities Protein Structure Tertiary Biochemistry Associated function Trans-Activators Carrier Proteins Sequence Alignment Two-dimensional nuclear magnetic resonance spectroscopy Heteronuclear single quantum coherence spectroscopy Protein Binding |
| Zdroj: | Journal of Molecular Biology. 362:287-297 |
| ISSN: | 0022-2836 |
| DOI: | 10.1016/j.jmb.2006.07.010 |
| Popis: | The 22 kDa haem-binding protein, p22HBP, is highly expressed in erythropoietic tissues and binds to a range of metallo- and non-metalloporphyrin molecules with similar affinities, suggesting a role in haem regulation or synthesis. We have determined the three-dimensional solution structure of p22HBP and mapped the porphyrin-binding site, which comprises a number of loops and a alpha-helix all located on a single face of the molecule. The structure of p22HBP is related to the bacterial multi-drug resistance protein BmrR, and is the first protein with this fold to be identified in eukaryotes. Strikingly, the porphyrin-binding site in p22HBP is located in a similar position to the drug-binding site of BmrR. These similarities suggest that the broad ligand specificity observed for both BmrR and p22HBP may result from a conserved ligand interaction mechanism. Taken together, these data suggest that the both the fold and its associated function, that of binding to a broad range of small hydrophobic molecules, are ancient, and have been adapted throughout evolution for a variety of purposes. |
| Databáze: | OpenAIRE |
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