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| | <StructureSection load='3gqg' size='340' side='right'caption='[[3gqg]], [[Resolution|resolution]] 1.73Å' scene=''> | | <StructureSection load='3gqg' size='340' side='right'caption='[[3gqg]], [[Resolution|resolution]] 1.73Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3gqg]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Trematomus_bernacchii Trematomus bernacchii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GQG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3GQG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3gqg]] is a 4 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=3GQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GQG FirstGlance]. <br> |
| - | </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></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.73Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></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'>[http://proteopedia.org/fgij/fg.htm?mol=3gqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gqg OCA], [http://pdbe.org/3gqg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gqg RCSB], [http://www.ebi.ac.uk/pdbsum/3gqg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3gqg ProSAT]</span></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=3gqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gqg OCA], [https://pdbe.org/3gqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gqg RCSB], [https://www.ebi.ac.uk/pdbsum/3gqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gqg ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HBA_TREBE HBA_TREBE]] Involved in oxygen transport from gills to the various peripheral tissues. [[http://www.uniprot.org/uniprot/HBB_TREBE HBB_TREBE]] Involved in oxygen transport from gills to the various peripheral tissues. | + | [https://www.uniprot.org/uniprot/HBA_TREBE HBA_TREBE] Involved in oxygen transport from gills to the various peripheral tissues. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Trematomus bernacchii]] | | [[Category: Trematomus bernacchii]] |
| - | [[Category: Bonomi, G]] | + | [[Category: Bonomi G]] |
| - | [[Category: Franzese, M]] | + | [[Category: Franzese M]] |
| - | [[Category: Mazzarella, L]] | + | [[Category: Mazzarella L]] |
| - | [[Category: Merlino, A]] | + | [[Category: Merlino A]] |
| - | [[Category: Vergara, A]] | + | [[Category: Vergara A]] |
| - | [[Category: Acetylation]]
| + | |
| - | [[Category: Antacrtic fish hemoglobin]]
| + | |
| - | [[Category: Heme]]
| + | |
| - | [[Category: Iron]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Oxygen transport]]
| + | |
| - | [[Category: Transport]]
| + | |
| Structural highlights
Function
HBA_TREBE Involved in oxygen transport from gills to the various peripheral tissues.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Oxidation of Hbs leads to the formation of different forms of Fe(III) that are relevant to a range of biochemical and physiological functions. Here we report a combined EPR/x-ray crystallography study performed at acidic pH on six ferric tetrameric Hbs. Five of the Hbs were isolated from the high-Antarctic notothenioid fishes Trematomus bernacchii, Trematomus newnesi, and Gymnodraco acuticeps, and one was isolated from the sub-Antarctic notothenioid Cottoperca gobio. Our EPR analysis reveals that 1), in all of these Hbs, at acidic pH the aquomet form and two hemichromes coexist; and 2), only in the three Hbs that exhibit the Root effect is a significant amount of the pentacoordinate (5C) high-spin Fe(III) form found. The crystal structure at acidic pH of the ferric form of the Root-effect Hb from T. bernacchii is also reported at 1.7 A resolution. This structure reveals a 5C state of the heme iron for both the alpha- and beta-chains within a T quaternary structure. Altogether, the spectroscopic and crystallographic results indicate that the Root effect and hemichrome stability at acidic pH are correlated in tetrameric Hbs. Furthermore, Antarctic fish Hbs exhibit higher peroxidase activity than mammalian and temperate fish Hbs, suggesting that a partial hemichrome state in tetrameric Hbs, unlike in monomeric Hbs, does not remove the need for protection from peroxide attack, in contrast to previous results from monomeric Hbs.
Correlation between hemichrome stability and the root effect in tetrameric hemoglobins.,Vergara A, Franzese M, Merlino A, Bonomi G, Verde C, Giordano D, di Prisco G, Lee HC, Peisach J, Mazzarella L Biophys J. 2009 Aug 5;97(3):866-74. PMID:19651045[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Vergara A, Franzese M, Merlino A, Bonomi G, Verde C, Giordano D, di Prisco G, Lee HC, Peisach J, Mazzarella L. Correlation between hemichrome stability and the root effect in tetrameric hemoglobins. Biophys J. 2009 Aug 5;97(3):866-74. PMID:19651045 doi:10.1016/j.bpj.2009.04.056
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