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[[Image:1v07.gif|left|200px]]
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{{STRUCTURE_1v07|  PDB=1v07  |  SCENE=  }}
'''CRYSTAL STRUCTURE OF THRE11VAL MUTANT OF THE NERVE TISSUE MINI-HEMOGLOBIN FROM THE NEMERTEAN WORM CEREBRATULUS LACTEUS'''


==CRYSTAL STRUCTURE OF ThrE11Val mutant of THE NERVE TISSUE MINI-HEMOGLOBIN FROM THE NEMERTEAN WORM CEREBRATULUS LACTEUS==
<StructureSection load='1v07' size='340' side='right'caption='[[1v07]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1v07]] 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=1V07 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V07 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]] 1.7&#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=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=1v07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v07 OCA], [https://pdbe.org/1v07 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v07 RCSB], [https://www.ebi.ac.uk/pdbsum/1v07 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v07 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/v0/1v07_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=1v07 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The mini-hemoglobin from Cerebratulus lacteus (CerHb) belongs to a class of globins containing the polar Tyr-B10/Gln-E7 amino acid pair that normally causes low rates of O2 dissociation and ultra-high O2 affinity, which suggest O2 sensing or NO scavenging functions. CerHb, however, has high rates of O2 dissociation (kO2 = 200-600 s(-1)) and moderate O2 affinity (KO2) approximately 1 microm(-1)) as a result of a third polar amino acid in its active site, Thr-E11. When Thr-E11 is replaced by Val, kO2 decreases 1000-fold and KO2 increases 130-fold at pH 7.0, 20 degrees C. The mutation also shifts the stretching frequencies of both heme-bound and photodissociated CO, indicating marked changes of the electrostatic field at the active site. The crystal structure of Thr-E11 --&gt; Val CerHbO2 at 1.70 A resolution is almost identical to that of the wild-type protein (root mean square deviation of 0.12 A). The dramatic functional and spectral effects of the Thr-E11 --&gt; Val mutation are due exclusively to changes in the hydrogen bonding network in the active site. Replacing Thr-E11 with Val "frees" the Tyr-B10 hydroxyl group to rotate toward and donate a strong hydrogen bond to the heme-bound ligand, causing a selective increase in O2 affinity, a decrease of the rate coefficient for O2 dissociation, a 40 cm(-1) decrease in nuCO of heme-bound CO, and an increase in ligand migration toward more remote intermediate sites.


==Overview==
Thr-E11 regulates O2 affinity in Cerebratulus lacteus mini-hemoglobin.,Pesce A, Nardini M, Ascenzi P, Geuens E, Dewilde S, Moens L, Bolognesi M, Riggs AF, Hale A, Deng P, Nienhaus GU, Olson JS, Nienhaus K J Biol Chem. 2004 Aug 6;279(32):33662-72. Epub 2004 May 25. PMID:15161908<ref>PMID:15161908</ref>
The mini-hemoglobin from Cerebratulus lacteus (CerHb) belongs to a class of globins containing the polar Tyr-B10/Gln-E7 amino acid pair that normally causes low rates of O2 dissociation and ultra-high O2 affinity, which suggest O2 sensing or NO scavenging functions. CerHb, however, has high rates of O2 dissociation (kO2 = 200-600 s(-1)) and moderate O2 affinity (KO2) approximately 1 microm(-1)) as a result of a third polar amino acid in its active site, Thr-E11. When Thr-E11 is replaced by Val, kO2 decreases 1000-fold and KO2 increases 130-fold at pH 7.0, 20 degrees C. The mutation also shifts the stretching frequencies of both heme-bound and photodissociated CO, indicating marked changes of the electrostatic field at the active site. The crystal structure of Thr-E11 --&gt; Val CerHbO2 at 1.70 A resolution is almost identical to that of the wild-type protein (root mean square deviation of 0.12 A). The dramatic functional and spectral effects of the Thr-E11 --&gt; Val mutation are due exclusively to changes in the hydrogen bonding network in the active site. Replacing Thr-E11 with Val "frees" the Tyr-B10 hydroxyl group to rotate toward and donate a strong hydrogen bond to the heme-bound ligand, causing a selective increase in O2 affinity, a decrease of the rate coefficient for O2 dissociation, a 40 cm(-1) decrease in nuCO of heme-bound CO, and an increase in ligand migration toward more remote intermediate sites.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1V07 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cerebratulus_lacteus Cerebratulus lacteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V07 OCA].
</div>
<div class="pdbe-citations 1v07" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Thr-E11 regulates O2 affinity in Cerebratulus lacteus mini-hemoglobin., Pesce A, Nardini M, Ascenzi P, Geuens E, Dewilde S, Moens L, Bolognesi M, Riggs AF, Hale A, Deng P, Nienhaus GU, Olson JS, Nienhaus K, J Biol Chem. 2004 Aug 6;279(32):33662-72. Epub 2004 May 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15161908 15161908]
*[[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: Deng, P.]]
[[Category: Deng P]]
[[Category: Dewilde, S.]]
[[Category: Dewilde S]]
[[Category: Geuens, E.]]
[[Category: Geuens E]]
[[Category: Hale, A.]]
[[Category: Hale A]]
[[Category: Moens, L.]]
[[Category: Moens L]]
[[Category: Nardini, M.]]
[[Category: Nardini M]]
[[Category: Nienhaus, G U.]]
[[Category: Nienhaus GU]]
[[Category: Nienhaus, K.]]
[[Category: Nienhaus K]]
[[Category: Olson, J S.]]
[[Category: Olson JS]]
[[Category: Pesce, A.]]
[[Category: Pesce A]]
[[Category: Riggs, A.]]
[[Category: Riggs A]]
[[Category: Nerve tissue mini-hemoglobin]]
[[Category: Oxygen affinity of c lacteus mini-hemoglobin]]
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