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A novel haem-binding interface in the 22 kDa haem-binding protein p22HBP
journal contribution
posted on 2023-05-17, 02:58 authored by David GellDavid Gell, Westman, BJ, Gorman, D, Liew, C, Welch, JJ, Weiss, MJ, Mackay, JPThe 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 α-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. © 2006 Elsevier Ltd. All rights reserved.
History
Publication title
Journal of Molecular BiologyVolume
362Pagination
287-297ISSN
0022-2836Department/School
Menzies Institute for Medical ResearchPublisher
Academic Press Ltd Elsevier Science LtdPlace of publication
24-28 Oval Rd, London, England, Nw1 7DxRepository Status
- Restricted