1kfr: Difference between revisions
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== | ==Structural plasticity in the eight-helix fold of a trematode hemoglobin== | ||
<StructureSection load='1kfr' size='340' side='right'caption='[[1kfr]], [[Resolution|resolution]] 1.85Å' 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]] 1.85Å</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. | 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. | ||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1kfr" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Paramphistomum epiclitum]] | [[Category: Paramphistomum epiclitum]] | ||
[[Category: Ascenzi P]] | |||
[[Category: Ascenzi | [[Category: Bolognesi M]] | ||
[[Category: Bolognesi | [[Category: Dewilde S]] | ||
[[Category: Dewilde | [[Category: Milani M]] | ||
[[Category: Milani | [[Category: Moens L]] | ||
[[Category: Moens | [[Category: Pesce A]] | ||
[[Category: Pesce | |||
Latest revision as of 06:23, 13 August 2026
Structural plasticity in the eight-helix fold of a trematode hemoglobin
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