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| | == Structural highlights == | | == Structural highlights == |
| | <table><tr><td colspan='2'>[[2zlu]] 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=2ZLU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZLU FirstGlance]. <br> | | <table><tr><td colspan='2'>[[2zlu]] 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=2ZLU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZLU 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]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1y8k|1y8k]], [[1y8i|1y8i]], [[1y8h|1y8h]], [[1lfq|1lfq]], [[1jy7|1jy7]], [[1lfl|1lfl]], [[2zlt|2zlt]], [[2zlv|2zlv]], [[2zlw|2zlw]], [[2zlx|2zlx]]</div></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zlu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zlu OCA], [https://pdbe.org/2zlu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zlu RCSB], [https://www.ebi.ac.uk/pdbsum/2zlu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zlu 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=2zlu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zlu OCA], [https://pdbe.org/2zlu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zlu RCSB], [https://www.ebi.ac.uk/pdbsum/2zlu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zlu ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/HBA_HORSE HBA_HORSE]] Involved in oxygen transport from the lung to the various peripheral tissues. [[https://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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Equus caballus]] | | [[Category: Equus caballus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kaushal, P S]] | + | [[Category: Kaushal PS]] |
| - | [[Category: Sankaranarayanan, R]] | + | [[Category: Sankaranarayanan R]] |
| - | [[Category: Vijayan, M]] | + | [[Category: Vijayan M]] |
| - | [[Category: Allosteric transition]]
| + | |
| - | [[Category: Heme]]
| + | |
| - | [[Category: Iron]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Oxygen storage]]
| + | |
| - | [[Category: Oxygen transport]]
| + | |
| - | [[Category: Polymorphism]]
| + | |
| - | [[Category: Protein hydration]]
| + | |
| - | [[Category: Solvent content and crystal structure]]
| + | |
| - | [[Category: Transport]]
| + | |
| - | [[Category: Variability in quaternary structure]]
| + | |
| - | [[Category: Water-mediated transformation]]
| + | |
| Structural highlights
Function
HBA_HORSE Involved in oxygen transport from the lung 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
The crystal structure of high-salt horse methaemoglobin has been determined at environmental relative humidities (r.h.) of 88, 79, 75 and 66%. The molecule is in the R state in the native and the r.h. 88% crystals. At r.h. 79%, the water content of the crystal is reduced and the molecule appears to move towards the R2 state. The crystals undergo a water-mediated transformation involving a doubling of one of the unit-cell parameters and an increase in water content when the environmental humidity is further reduced to r.h. 75%. The water content is now similar to that in the native crystals and the molecules are in the R state. The crystal structure at r.h. 66% is similar, but not identical, to that at r.h. 75%, but the solvent content is substantially reduced and the molecules have a quaternary structure that is in between those corresponding to the R and R2 states. Thus, variation in hydration leads to variation in the quaternary structure. Furthermore, partial dehydration appears to shift the structure from the R state to the R2 state. This observation is in agreement with the earlier conclusion that the changes in protein structure that accompany partial dehydration are similar to those that occur during protein action.
Water-mediated variability in the structure of relaxed-state haemoglobin.,Kaushal PS, Sankaranarayanan R, Vijayan M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jun 1;64(Pt, 6):463-9. Epub 2008 May 17. PMID:18540052[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kaushal PS, Sankaranarayanan R, Vijayan M. Water-mediated variability in the structure of relaxed-state haemoglobin. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jun 1;64(Pt, 6):463-9. Epub 2008 May 17. PMID:18540052 doi:http://dx.doi.org/10.1107/S1744309108013109
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