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| | <StructureSection load='3gkv' size='340' side='right'caption='[[3gkv]], [[Resolution|resolution]] 1.40Å' scene=''> | | <StructureSection load='3gkv' size='340' side='right'caption='[[3gkv]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3gkv]] is a 2 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=3GKV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3GKV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3gkv]] 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=3GKV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GKV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <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]] 1.4Å</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=CMO:CARBON+MONOXIDE'>CMO</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=3gkv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gkv OCA], [http://pdbe.org/3gkv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gkv RCSB], [http://www.ebi.ac.uk/pdbsum/3gkv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3gkv 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=3gkv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gkv OCA], [https://pdbe.org/3gkv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gkv RCSB], [https://www.ebi.ac.uk/pdbsum/3gkv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gkv 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: Mazzarella, L]] | + | [[Category: Mazzarella L]] |
| - | [[Category: Merlino, A]] | + | [[Category: Merlino A]] |
| - | [[Category: Sica, F]] | + | [[Category: Sica F]] |
| - | [[Category: Vergara, A]] | + | [[Category: Vergara A]] |
| - | [[Category: Vitagliano, L]] | + | [[Category: Vitagliano L]] |
| - | [[Category: Acetylation]]
| + | |
| - | [[Category: Heme]]
| + | |
| - | [[Category: Hemoglobin]]
| + | |
| - | [[Category: Intermediate quaternary structure]]
| + | |
| - | [[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
Recent studies have demonstrated that hemoglobins isolated from Antarctic fish undergo peculiar oxidation processes. Here we show, by combining crystallographic and spectroscopic data, that the oxidation pathway of Trematomus bernacchii hemoglobin (HbTb) is distinct from that observed for the major component of Trematomus newnesi (Hb1Tn), despite the high sequence identity of the two proteins and structural similarity of their ferrous and fully oxidized states. Resonance Raman analysis of HbTb autoxidation upon air-exposure reveals the absence of the oxidized pentacoordinated state that was observed for Hb1Tn. The HbTb oxidation pathway is characterized by two ferric species: an aquo hexacoordinated high spin state and a bis-histidyl hexacoordinated low spin form, which appear in the early stages of the oxidation process. The high resolution structure of an intermediate along the oxidation pathway has been determined at 1.4 A resolution. The analysis of the electron density of the heme pocket shows, for both the alpha and the beta iron, the coexistence of multiple binding states. In this partially oxidized form, HbTb exhibits significant deviations from the canonical R state both at the local and global level. The analysis of these modifications highlights the structural correlation between key functional regions of the protein. (c) 2009 Wiley Periodicals, Inc. Biopolymers, 2009.
Combined crystallographic and spectroscopic analysis of Trematomus bernacchii hemoglobin highlights analogies and differences in the peculiar oxidation pathway of Antarctic fish hemoglobins.,Merlino A, Vitagliano L, Howes BD, Verde C, di Prisco G, Smulevich G, Sica F, Vergara A Biopolymers. 2009 Apr 16. PMID:19373928[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Merlino A, Vitagliano L, Howes BD, Verde C, di Prisco G, Smulevich G, Sica F, Vergara A. Combined crystallographic and spectroscopic analysis of Trematomus bernacchii hemoglobin highlights analogies and differences in the peculiar oxidation pathway of Antarctic fish hemoglobins. Biopolymers. 2009 Apr 16. PMID:19373928 doi:10.1002/bip.21206
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