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New page: left|200px<br /> <applet load="1kr7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kr7, resolution 1.5Å" /> '''Crystal structure of...
 
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[[Image:1kr7.gif|left|200px]]<br />
<applet load="1kr7" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1kr7, resolution 1.5&Aring;" />
'''Crystal structure of the nerve tissue mini-hemoglobin from the nemertean worm Cerebratulus lacteus'''<br />


==Overview==
==Crystal structure of the nerve tissue mini-hemoglobin from the nemertean worm Cerebratulus lacteus==
A very short hemoglobin (CerHb; 109 amino acids) binds O(2) cooperatively, in the nerve tissue of the nemertean worm Cerebratulus lacteus to sustain, neural activity during anoxia. Sequence analysis suggests that CerHb, tertiary structure may be unique among the known globin fold evolutionary, variants. The X-ray structure of oxygenated CerHb (R factor 15.3%, at 1.5, A resolution) displays deletion of the globin N-terminal A helix, an, extended GH region, a very short H helix, and heme solvent shielding based, on specific aromatic residues. The heme-bound O(2) is stabilized by, hydrogen bonds to the distal TyrB10-GlnE7 pair. Ligand access to heme may, take place through a wide protein matrix tunnel connecting the distal site, to a surface cleft located between the E and H helices.
<StructureSection load='1kr7' size='340' side='right'caption='[[1kr7]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1kr7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cerebratulus_lacteus Cerebratulus lacteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KR7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KR7 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]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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=1kr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kr7 OCA], [https://pdbe.org/1kr7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kr7 RCSB], [https://www.ebi.ac.uk/pdbsum/1kr7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kr7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GLBN_CERLA GLBN_CERLA] Acts as an oxygen store capable of sustaining neuronal activity in an anoxic environment for 5 to 30 min.
== 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/kr/1kr7_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=1kr7 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A very short hemoglobin (CerHb; 109 amino acids) binds O(2) cooperatively in the nerve tissue of the nemertean worm Cerebratulus lacteus to sustain neural activity during anoxia. Sequence analysis suggests that CerHb tertiary structure may be unique among the known globin fold evolutionary variants. The X-ray structure of oxygenated CerHb (R factor 15.3%, at 1.5 A resolution) displays deletion of the globin N-terminal A helix, an extended GH region, a very short H helix, and heme solvent shielding based on specific aromatic residues. The heme-bound O(2) is stabilized by hydrogen bonds to the distal TyrB10-GlnE7 pair. Ligand access to heme may take place through a wide protein matrix tunnel connecting the distal site to a surface cleft located between the E and H helices.


==About this Structure==
The 109 residue nerve tissue minihemoglobin from Cerebratulus lacteus highlights striking structural plasticity of the alpha-helical globin fold.,Pesce A, Nardini M, Dewilde S, Geuens E, Yamauchi K, Ascenzi P, Riggs AF, Moens L, Bolognesi M Structure. 2002 May;10(5):725-35. PMID:12015154<ref>PMID:12015154</ref>
1KR7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cerebratulus_lacteus Cerebratulus lacteus] with SO4, ACT, HEM and OXY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KR7 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
The 109 residue nerve tissue minihemoglobin from Cerebratulus lacteus highlights striking structural plasticity of the alpha-helical globin fold., Pesce A, Nardini M, Dewilde S, Geuens E, Yamauchi K, Ascenzi P, Riggs AF, Moens L, Bolognesi M, Structure. 2002 May;10(5):725-35. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12015154 12015154]
</div>
<div class="pdbe-citations 1kr7" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cerebratulus lacteus]]
[[Category: Cerebratulus lacteus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Ascenzi, P.]]
[[Category: Ascenzi P]]
[[Category: Bolognesi, M.]]
[[Category: Bolognesi M]]
[[Category: Dewilde, S.]]
[[Category: Dewilde S]]
[[Category: Geuens, E.]]
[[Category: Geuens E]]
[[Category: Moens, L.]]
[[Category: Moens L]]
[[Category: Nardini, M.]]
[[Category: Nardini M]]
[[Category: Pesce, A.]]
[[Category: Pesce A]]
[[Category: Riggs, A.F.]]
[[Category: Riggs AF]]
[[Category: Yamauchi, k.]]
[[Category: Yamauchi k]]
[[Category: ACT]]
[[Category: HEM]]
[[Category: OXY]]
[[Category: SO4]]
[[Category: mini-hemoglobin]]
[[Category: nerve tissue]]
[[Category: oxygen transport]]
[[Category: protein cavities]]
 
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