2hva

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[[Image:2hva.gif|left|200px]]
 
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{{Structure
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==Solution Structure of the haem-binding protein p22HBP==
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|PDB= 2hva |SIZE=350|CAPTION= <scene name='initialview01'>2hva</scene>
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<StructureSection load='2hva' size='340' side='right'caption='[[2hva]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE= Hebp1, Hbp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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<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>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<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://www.ebi.ac.uk/pdbsum/2hva PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hva RCSB]</span>
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[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>
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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'''Solution Structure of the haem-binding protein p22HBP'''
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hv/2hva_consurf.spt"</scriptWhenChecked>
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==Overview==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2hva ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== 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.
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.
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==About this Structure==
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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<ref>PMID:16905148</ref>
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2HVA is a [[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].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16905148 16905148]
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</div>
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<div class="pdbe-citations 2hva" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Gell DA]]
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[[Category: Gell, D A.]]
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[[Category: Gorman D]]
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[[Category: Gorman, D.]]
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[[Category: Liew CK]]
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[[Category: Liew, C K.]]
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[[Category: Mackay JP]]
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[[Category: Mackay, J P.]]
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[[Category: Westman BJ]]
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[[Category: Westman, B J.]]
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[[Category: beta-beta-alpha-beta-beta repeat]]
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[[Category: haem-binding protein]]
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[[Category: hydrophobic-ligand binding domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:35:54 2008''
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Current revision

Solution Structure of the haem-binding protein p22HBP

PDB ID 2hva

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