This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2hva

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(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...)
Current revision (19:03, 29 May 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2hva.gif|left|200px]]<br /><applet load="2hva" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="2hva" />
 
-
'''Solution Structure of the haem-binding protein p22HBP'''<br />
 
-
==Overview==
+
==Solution Structure of the haem-binding protein p22HBP==
-
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.
+
<StructureSection load='2hva' size='340' side='right'caption='[[2hva]]' scene=''>
 +
== Structural highlights ==
 +
<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='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=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 ==
 +
[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]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hv/2hva_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== 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.
-
==About this Structure==
+
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>
-
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 superseeds the now removed PDB entry 2HC6. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HVA OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16905148 16905148]
+
</div>
 +
<div class="pdbe-citations 2hva" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
-
[[Category: Single protein]]
+
[[Category: Gell DA]]
-
[[Category: Gell, D.A.]]
+
[[Category: Gorman D]]
-
[[Category: Gorman, D.]]
+
[[Category: Liew CK]]
-
[[Category: Liew, C.K.]]
+
[[Category: Mackay JP]]
-
[[Category: Mackay, J.P.]]
+
[[Category: Westman BJ]]
-
[[Category: Westman, B.J.]]
+
-
[[Category: beta-beta-alpha-beta-beta repeat]]
+
-
[[Category: haem-binding protein]]
+
-
[[Category: hydrophobic-ligand binding domain]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:00:23 2007''
+

Current revision

Solution Structure of the haem-binding protein p22HBP

PDB ID 2hva

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools