2hva
From Proteopedia
(New page: 200px<br /><applet load="2hva" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hva" /> '''Solution Structure of the haem-binding prote...) |
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'''Solution Structure of the haem-binding protein p22HBP'''<br /> | '''Solution Structure of the haem-binding protein p22HBP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The 22 kDa haem-binding protein, p22HBP, is highly expressed in | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 2HVA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure | + | 2HVA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry 2HC6. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HVA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Gell, D | + | [[Category: Gell, D A.]] |
[[Category: Gorman, D.]] | [[Category: Gorman, D.]] | ||
| - | [[Category: Liew, C | + | [[Category: Liew, C K.]] |
| - | [[Category: Mackay, J | + | [[Category: Mackay, J P.]] |
| - | [[Category: Westman, B | + | [[Category: Westman, B J.]] |
[[Category: beta-beta-alpha-beta-beta repeat]] | [[Category: beta-beta-alpha-beta-beta repeat]] | ||
[[Category: haem-binding protein]] | [[Category: haem-binding protein]] | ||
[[Category: hydrophobic-ligand binding domain]] | [[Category: hydrophobic-ligand binding domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:46:07 2008'' |
Revision as of 15:46, 21 February 2008
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Solution Structure of the haem-binding protein p22HBP
Overview
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.
About this Structure
2HVA is a Single protein structure of sequence from Mus musculus. This structure supersedes the now removed PDB entry 2HC6. Full crystallographic information is available from OCA.
Reference
A novel haem-binding interface in the 22 kDa haem-binding protein p22HBP., Gell DA, Westman BJ, Gorman D, Liew C, Welch JJ, Weiss MJ, Mackay JP, J Mol Biol. 2006 Sep 15;362(2):287-97. Epub 2006 Aug 14. PMID:16905148
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