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| | ==Solution structure of Murine p22HBP== | | ==Solution structure of Murine p22HBP== |
| - | <StructureSection load='2gov' size='340' side='right'caption='[[2gov]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2gov' size='340' side='right'caption='[[2gov]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2gov]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GOV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GOV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2gov]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GOV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GOV FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Hebp1, Hbp ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=2gov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gov OCA], [https://pdbe.org/2gov PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gov RCSB], [https://www.ebi.ac.uk/pdbsum/2gov PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gov ProSAT], [https://www.topsan.org/Proteins/CESG/2gov TOPSAN]</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=2gov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gov OCA], [https://pdbe.org/2gov PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gov RCSB], [https://www.ebi.ac.uk/pdbsum/2gov PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gov ProSAT], [https://www.topsan.org/Proteins/CESG/2gov TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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>
| + | [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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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Dias JS]] |
| - | [[Category: Dias, J S]] | + | [[Category: Goodfellow BJ]] |
| - | [[Category: Goodfellow, B J]] | + | [[Category: Peterson FC]] |
| - | [[Category: Peterson, F C]] | + | [[Category: Volkman BF]] |
| - | [[Category: Volkman, B F]] | + | |
| - | [[Category: Cesg]]
| + | |
| - | [[Category: Heme binding]]
| + | |
| - | [[Category: Heme binding protein]]
| + | |
| - | [[Category: P22hbp]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| 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
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.
The first structure from the SOUL/HBP family of heme-binding proteins, murine P22HBP.,Dias JS, Macedo AL, Ferreira GC, Peterson FC, Volkman BF, Goodfellow BJ J Biol Chem. 2006 Oct 20;281(42):31553-61. Epub 2006 Aug 10. PMID:16905545[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
- ↑ 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
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