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[[Image:1kfr.jpg|left|200px]]
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{{STRUCTURE_1kfr|  PDB=1kfr  |  SCENE=  }}
'''Structural plasticity in the eight-helix fold of a trematode hemoglobin'''


==Structural plasticity in the eight-helix fold of a trematode hemoglobin==
<StructureSection load='1kfr' size='340' side='right'caption='[[1kfr]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1kfr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paramphistomum_epiclitum Paramphistomum epiclitum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KFR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1kfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfr OCA], [https://pdbe.org/1kfr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kfr RCSB], [https://www.ebi.ac.uk/pdbsum/1kfr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GLB_PAREP GLB_PAREP] Oxygen binding protein.
== 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/kf/1kfr_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1kfr ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional structure of recombinant haemoglobin from the trematode Paramphistomum epiclitum, displaying the highest oxygen affinity so far observed for (non)vertebrate haemoglobins, has previously been determined at 1.17 A resolution (orthorhombic space group P2(1)2(1)2(1)). In the present communication, the three-dimensional structure of wild-type P. epiclitum haemoglobin is reported at 1.85 A resolution in a monoclinic crystal form (R factor = 16.1%, R(free) = 22.0%). Comparison of P. epiclitum (recombinant versus wild-type ferric Hb) structures in the two crystal forms shows structural differences in the haem proximal and distal sites which have not been reported for other known haemoglobin structures previously.


==Overview==
Structural plasticity in the eight-helix fold of a trematode haemoglobin.,Milani M, Pesce A, Dewilde S, Ascenzi P, Moens L, Bolognesi M Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):719-22. Epub 2002, Mar 22. PMID:11914507<ref>PMID:11914507</ref>
The three-dimensional structure of recombinant haemoglobin from the trematode Paramphistomum epiclitum, displaying the highest oxygen affinity so far observed for (non)vertebrate haemoglobins, has previously been determined at 1.17 A resolution (orthorhombic space group P2(1)2(1)2(1)). In the present communication, the three-dimensional structure of wild-type P. epiclitum haemoglobin is reported at 1.85 A resolution in a monoclinic crystal form (R factor = 16.1%, R(free) = 22.0%). Comparison of P. epiclitum (recombinant versus wild-type ferric Hb) structures in the two crystal forms shows structural differences in the haem proximal and distal sites which have not been reported for other known haemoglobin structures previously.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1KFR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Paramphistomum_epiclitum Paramphistomum epiclitum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFR OCA].
</div>
<div class="pdbe-citations 1kfr" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structural plasticity in the eight-helix fold of a trematode haemoglobin., Milani M, Pesce A, Dewilde S, Ascenzi P, Moens L, Bolognesi M, Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):719-22. Epub 2002, Mar 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11914507 11914507]
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Paramphistomum epiclitum]]
[[Category: Paramphistomum epiclitum]]
[[Category: Single protein]]
[[Category: Ascenzi P]]
[[Category: Ascenzi, P.]]
[[Category: Bolognesi M]]
[[Category: Bolognesi, M.]]
[[Category: Dewilde S]]
[[Category: Dewilde, S.]]
[[Category: Milani M]]
[[Category: Milani, M.]]
[[Category: Moens L]]
[[Category: Moens, L.]]
[[Category: Pesce A]]
[[Category: Pesce, A.]]
[[Category: Hemoglobin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 22:41:30 2008''

Latest revision as of 06:23, 13 August 2026

Structural plasticity in the eight-helix fold of a trematode hemoglobin

1kfr, resolution 1.85Å

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