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[[Image:1kfr.jpg|left|200px]]<br /><applet load="1kfr" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1kfr, resolution 1.85&Aring;" />
'''Structural plasticity in the eight-helix fold of a trematode hemoglobin'''<br />


==Overview==
==Structural plasticity in the eight-helix fold of a trematode hemoglobin==
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.
<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/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=1kfr ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1KFR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paramphistomum_epiclitum Paramphistomum epiclitum] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFR OCA].
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11914507 11914507]
[[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: HEM]]
[[Category: SO4]]
[[Category: hemoglobin]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:13:13 2008''

Latest revision as of 10:46, 7 February 2024

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

Structural highlights

1kfr is a 1 chain structure with sequence from Paramphistomum epiclitum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.85Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GLB_PAREP Oxygen binding protein.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1kfr, resolution 1.85Å

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