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2hva

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Revision as of 07:22, 24 March 2021

Solution Structure of the haem-binding protein p22HBP

Structural highlights

2hva is a 1 chain structure with sequence from Lk3 transgenic mice. This structure supersedes the now removed PDB entry 2hc6. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	Hebp1, Hbp (LK3 transgenic mice)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2hva"

@@ Line 1: / Line 1: @@
 ==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]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''>
 == 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/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 [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='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>
-<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>
 == 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Lk3 transgenic mice]]
 [[Category: Gell, D A]]

2hva

From Proteopedia

Revision as of 07:22, 24 March 2021

Solution Structure of the haem-binding protein p22HBP

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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