View source for 2peg


==Crystal structure of Trematomus bernacchii hemoglobin in a partial hemichrome state==
<StructureSection load='2peg' size='340' side='right'caption='[[2peg]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2peg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trematomus_bernacchii Trematomus bernacchii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PEG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PEG 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]] 1.48&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=2peg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2peg OCA], [https://pdbe.org/2peg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2peg RCSB], [https://www.ebi.ac.uk/pdbsum/2peg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2peg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HBA_TREBE HBA_TREBE] Involved in oxygen transport from gills to the various peripheral tissues.
== 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/pe/2peg_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=2peg ConSurf].
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Spontaneous autoxidation of tetrameric Hbs leads to the formation of Fe (III) forms, whose physiological role is not fully understood. Here we report structural characterization by EPR of the oxidized states of tetrameric Hbs isolated from the Antarctic fish species Trematomus bernacchii, Trematomus newnesi, and Gymnodraco acuticeps, as well as the x-ray crystal structure of oxidized Trematomus bernacchii Hb, redetermined at high resolution. The oxidation of these Hbs leads to formation of states that were not usually detected in previous analyses of tetrameric Hbs. In addition to the commonly found aquo-met and hydroxy-met species, EPR analyses show that two distinct hemichromes coexist at physiological pH, referred to as hemichromes I and II, respectively. Together with the high-resolution crystal structure (1.5 A) of T. bernacchii and a survey of data available for other heme proteins, hemichrome I was assigned by x-ray crystallography and by EPR as a bis-His complex with a distorted geometry, whereas hemichrome II is a less constrained (cytochrome b5-like) bis-His complex. In four of the five Antartic fish Hbs examined, hemichrome I is the major form. EPR shows that for HbCTn, the amount of hemichrome I is substantially reduced. In addition, the concomitant presence of a penta-coordinated high-spin Fe (III) species, to our knowledge never reported before for a wild-type tetrameric Hb, was detected. A molecular modeling investigation demonstrates that the presence of the bulkier Ile in position 67beta in HbCTn in place of Val as in the other four Hbs impairs the formation of hemichrome I, thus favoring the formation of the ferric penta-coordinated species. Altogether the data show that ferric states commonly associated with monomeric and dimeric Hbs are also found in tetrameric Hbs.

Structural characterization of ferric hemoglobins from three antarctic fish species of the suborder notothenioidei.,Vergara A, Franzese M, Merlino A, Vitagliano L, Verde C, di Prisco G, Lee HC, Peisach J, Mazzarella L Biophys J. 2007 Oct 15;93(8):2822-9. Epub 2007 Jun 1. PMID:17545238<ref>PMID:17545238</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2peg" style="background-color:#fffaf0;"></div>

==See Also==
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Trematomus bernacchii]]
[[Category: Franzese M]]
[[Category: Mazzarella L]]
[[Category: Merlino A]]
[[Category: Vergara A]]
[[Category: Vitagliano L]]