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| | <StructureSection load='3mkb' size='340' side='right'caption='[[3mkb]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='3mkb' size='340' side='right'caption='[[3mkb]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3mkb]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Isurus_oxyrinchus Isurus oxyrinchus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MKB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MKB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3mkb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Isurus_oxyrinchus Isurus oxyrinchus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MKB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MKB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 1.9Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gcv|1gcv]], [[1gcw|1gcw]]</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=3mkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mkb OCA], [https://pdbe.org/3mkb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mkb RCSB], [https://www.ebi.ac.uk/pdbsum/3mkb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mkb ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3mkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mkb OCA], [http://pdbe.org/3mkb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mkb RCSB], [http://www.ebi.ac.uk/pdbsum/3mkb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mkb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/F2Z286_ISUOX F2Z286_ISUOX] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Isurus oxyrinchus]] | | [[Category: Isurus oxyrinchus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Balasubramanian, M]] | + | [[Category: Balasubramanian M]] |
| - | [[Category: Moorthy, P Sathya]]
| + | [[Category: Ponnuswamy MN]] |
| - | [[Category: Ponnuswamy, M N]] | + | [[Category: Ramesh P]] |
| - | [[Category: Ramesh, P]] | + | [[Category: Sathya Moorthy P]] |
| - | [[Category: Sundaresan, S S]] | + | [[Category: Sundaresan SS]] |
| - | [[Category: Hemoglobin]] | + | |
| - | [[Category: Oxygen affinity]]
| + | |
| - | [[Category: Oxygen storage]]
| + | |
| - | [[Category: Oxygen transport]]
| + | |
| - | [[Category: Shortfin mako]]
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| Structural highlights
Function
F2Z286_ISUOX
Publication Abstract from PubMed
Haemoglobin (Hb) is a tetrameric iron-containing protein that carries oxygen from the lungs to tissues and carbon dioxide from tissues back to the lungs. Pisces are the advanced aquatic vertebrates capable of surviving at wide depth ranges. The shortfin mako shark (SMS) is the pelagic, largest, fastest and most sophisticated species of the shark kingdom with well developed eyes. Mostly the pisces species are cold blooded in nature. Distinctly, the SMSs are warm-blooded animals with an advanced circulatory system. SMSs are capable of maintaining elevated muscle temperatures up to 33 K above the ambient water temperatures at a depth of 150-500 m. SMSs have a diverged air-breathing mechanism compared with other vertebrates. The haemoglobin molecule consists of four polypeptide chains, namely two alpha chains, each with 140 amino acids and two beta chains each having 136 amino acids. The SMS Hb was found to crystallize in monoclinic space group P21 using the hanging-drop vapour-diffusion method at room temperature. The crystal packing parameters for the SMS Hb structure contain one whole biological molecule in the asymmetric unit with a solvent content of 47%. The SMS Hb quaternary structural features interface-interface interactions and heme binding sites are discussed with different state Hbs and the results reveal that SMS Hb adopts an unliganded deoxy T state conformation.
Structural studies of haemoglobin from pisces species shortfin mako shark (Isurus oxyrinchus) at 1.9 A resolution.,Ramesh P, Sundaresan SS, Sathya Moorthy P, Balasubramanian M, Ponnuswamy MN J Synchrotron Radiat. 2013 Nov;20(Pt 6):843-7. doi: 10.1107/S0909049513021572., Epub 2013 Oct 1. PMID:24121325[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ramesh P, Sundaresan SS, Sathya Moorthy P, Balasubramanian M, Ponnuswamy MN. Structural studies of haemoglobin from pisces species shortfin mako shark (Isurus oxyrinchus) at 1.9 A resolution. J Synchrotron Radiat. 2013 Nov;20(Pt 6):843-7. doi: 10.1107/S0909049513021572., Epub 2013 Oct 1. PMID:24121325 doi:http://dx.doi.org/10.1107/S0909049513021572
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