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| | ==Solution Structure of the haem-binding protein p22HBP== | | ==Solution Structure of the haem-binding protein p22HBP== |
| - | <StructureSection load='2hva' size='340' side='right' caption='[[2hva]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''> | + | <StructureSection load='2hva' size='340' side='right'caption='[[2hva]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2hva]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2hc6 2hc6]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HVA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HVA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2hva]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2hc6 2hc6]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HVA FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Hebp1, Hbp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hva OCA], [http://pdbe.org/2hva PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hva RCSB], [http://www.ebi.ac.uk/pdbsum/2hva PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hva ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hva OCA], [https://pdbe.org/2hva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hva RCSB], [https://www.ebi.ac.uk/pdbsum/2hva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hva ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HEBP1_MOUSE HEBP1_MOUSE]] May bind free porphyrinogens that may be present in the cell and thus facilitate removal of these potentially toxic compound. Binds with a high affinity to one molecule of heme or porphyrins. It binds metalloporphyrins, free porphyrins and N-methylprotoporphyrin with similar affinities.<ref>PMID:12413491</ref> <ref>PMID:16905545</ref> | + | [https://www.uniprot.org/uniprot/HEBP1_MOUSE HEBP1_MOUSE] May bind free porphyrinogens that may be present in the cell and thus facilitate removal of these potentially toxic compound. Binds with a high affinity to one molecule of heme or porphyrins. It binds metalloporphyrins, free porphyrins and N-methylprotoporphyrin with similar affinities.<ref>PMID:12413491</ref> <ref>PMID:16905545</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Gell, D A]] | + | [[Category: Mus musculus]] |
| - | [[Category: Gorman, D]] | + | [[Category: Gell DA]] |
| - | [[Category: Liew, C K]] | + | [[Category: Gorman D]] |
| - | [[Category: Mackay, J P]] | + | [[Category: Liew CK]] |
| - | [[Category: Westman, B J]] | + | [[Category: Mackay JP]] |
| - | [[Category: Beta-beta-alpha-beta-beta repeat]] | + | [[Category: Westman BJ]] |
| - | [[Category: Haem-binding protein]]
| + | |
| - | [[Category: Hydrophobic-ligand binding domain]]
| + | |
| - | [[Category: Ligand binding protein]]
| + | |
| Structural highlights
Function
HEBP1_MOUSE May bind free porphyrinogens that may be present in the cell and thus facilitate removal of these potentially toxic compound. Binds with a high affinity to one molecule of heme or porphyrins. It binds metalloporphyrins, free porphyrins and N-methylprotoporphyrin with similar affinities.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jacob Blackmon B, Dailey TA, Lianchun X, Dailey HA. Characterization of a human and mouse tetrapyrrole-binding protein. Arch Biochem Biophys. 2002 Nov 15;407(2):196-201. PMID:12413491
- ↑ Dias JS, Macedo AL, Ferreira GC, Peterson FC, Volkman BF, Goodfellow BJ. The first structure from the SOUL/HBP family of heme-binding proteins, murine P22HBP. J Biol Chem. 2006 Oct 20;281(42):31553-61. Epub 2006 Aug 10. PMID:16905545 doi:10.1074/jbc.M605988200
- ↑ Gell DA, Westman BJ, Gorman D, Liew C, Welch JJ, Weiss MJ, Mackay JP. A novel haem-binding interface in the 22 kDa haem-binding protein p22HBP. J Mol Biol. 2006 Sep 15;362(2):287-97. Epub 2006 Aug 14. PMID:16905148 doi:10.1016/j.jmb.2006.07.010
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