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| | <StructureSection load='5c6e' size='340' side='right'caption='[[5c6e]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='5c6e' size='340' side='right'caption='[[5c6e]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5c6e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C6E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C6E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5c6e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C6E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C6E FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</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">Hybrid , Neutron Diffraction , X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5c8i|5c8i]], [[5ccd|5ccd]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5c6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6e OCA], [http://pdbe.org/5c6e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c6e RCSB], [http://www.ebi.ac.uk/pdbsum/5c6e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c6e 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=5c6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6e OCA], [https://pdbe.org/5c6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c6e RCSB], [https://www.ebi.ac.uk/pdbsum/5c6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c6e ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HBA_HORSE HBA_HORSE]] Involved in oxygen transport from the lung to the various peripheral tissues. [[http://www.uniprot.org/uniprot/HBB_HORSE HBB_HORSE]] Involved in oxygen transport from the lung to the various peripheral tissues. | + | [https://www.uniprot.org/uniprot/HBA_HORSE HBA_HORSE] Involved in oxygen transport from the lung to the various peripheral tissues. |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Neutron crystallography provides direct visual evidence of the atomic positions of deuterium-exchanged H atoms, enabling the accurate determination of the protonation/deuteration state of hydrated biomolecules. Comparison of two neutron structures of hemoglobins, human deoxyhemoglobin (T state) and equine cyanomethemoglobin (R state), offers a direct observation of histidine residues that are likely to contribute to the Bohr effect. Previous studies have shown that the T-state N-terminal and C-terminal salt bridges appear to have a partial instead of a primary overall contribution. Four conserved histidine residues [alphaHis72(EF1), alphaHis103(G10), alphaHis89(FG1), alphaHis112(G19) and betaHis97(FG4)] can become protonated/deuterated from the R to the T state, while two histidine residues [alphaHis20(B1) and betaHis117(G19)] can lose a proton/deuteron. alphaHis103(G10), located in the alpha1:beta1 dimer interface, appears to be a Bohr group that undergoes structural changes: in the R state it is singly protonated/deuterated and hydrogen-bonded through a water network to betaAsn108(G10) and in the T state it is doubly protonated/deuterated with the network uncoupled. The very long-term H/D exchange of the amide protons identifies regions that are accessible to exchange as well as regions that are impermeable to exchange. The liganded relaxed state (R state) has comparable levels of exchange (17.1% non-exchanged) compared with the deoxy tense state (T state; 11.8% non-exchanged). Interestingly, the regions of non-exchanged protons shift from the tetramer interfaces in the T-state interface (alpha1:beta2 and alpha2:beta1) to the cores of the individual monomers and to the dimer interfaces (alpha1:beta1 and alpha2:beta2) in the R state. The comparison of regions of stability in the two states allows a visualization of the conservation of fold energy necessary for ligand binding and release.
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| - | Visualizing the Bohr effect in hemoglobin: neutron structure of equine cyanomethemoglobin in the R state and comparison with human deoxyhemoglobin in the T state.,Dajnowicz S, Seaver S, Hanson BL, Fisher SZ, Langan P, Kovalevsky AY, Mueser TC Acta Crystallogr D Struct Biol. 2016 Jul 1;72(Pt 7):892-903. doi:, 10.1107/S2059798316009049. Epub 2016 Jun 28. PMID:27377386<ref>PMID:27377386</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 5c6e" style="background-color:#fffaf0;"></div>
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| | | | |
| | ==See Also== | | ==See Also== |
| | *[[Hemoglobin 3D structures|Hemoglobin 3D structures]] | | *[[Hemoglobin 3D structures|Hemoglobin 3D structures]] |
| - | == References == | |
| - | <references/> | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Equus caballus]] | | [[Category: Equus caballus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dajnowicz, S]] | + | [[Category: Dajnowicz S]] |
| - | [[Category: Fisher, S Z]] | + | [[Category: Fisher SZ]] |
| - | [[Category: Hanson, B L]] | + | [[Category: Hanson BL]] |
| - | [[Category: Kovalevsky, A Y]] | + | [[Category: Kovalevsky AY]] |
| - | [[Category: Langan, P]] | + | [[Category: Langan P]] |
| - | [[Category: Mueser, T C]] | + | [[Category: Mueser TC]] |
| - | [[Category: Sean, S]] | + | [[Category: Sean S]] |
| - | [[Category: Equine hemoglobin]]
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| - | [[Category: Oxygen transport]]
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| - | [[Category: R-state]]
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