3d1a: Difference between revisions

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==Crystal Structure Determination of Goat Hemoglobin at 2.61 Angstrom Resolution==
==Crystal Structure Determination of Goat Hemoglobin at 2.61 Angstrom Resolution==
<StructureSection load='3d1a' size='340' side='right' caption='[[3d1a]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
<StructureSection load='3d1a' size='340' side='right'caption='[[3d1a]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3d1a]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Capra_hircus Capra hircus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D1A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3D1A FirstGlance]. <br>
<table><tr><td colspan='2'>[[3d1a]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Capra_hircus Capra hircus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D1A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D1A 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]] 2.61&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ri4|2ri4]], [[2qu0|2qu0]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3d1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d1a OCA], [http://pdbe.org/3d1a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3d1a RCSB], [http://www.ebi.ac.uk/pdbsum/3d1a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3d1a 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=3d1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d1a OCA], [https://pdbe.org/3d1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d1a RCSB], [https://www.ebi.ac.uk/pdbsum/3d1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d1a ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/HBBA_CAPHI HBBA_CAPHI]] Involved in oxygen transport from the lung to the various peripheral tissues.  
[https://www.uniprot.org/uniprot/HBA1_CAPHI HBA1_CAPHI] Involved in oxygen transport from the lung to the various peripheral tissues. Hemopressin acts as an antagonist peptide of the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and subsequent signaling.[UniProtKB:P01946]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d1/3d1a_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d1/3d1a_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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Haemoglobin is a tetrameric protein that plays a vital role in the transport of oxygen from the lungs to the tissues and of carbon dioxide back to the lungs. Even though a large amount of work has already been performed in this area, the study of the haemoglobin structures of avian and mammalian species is rather incomplete. Efforts are being made to understand the salient features of the species mentioned above. Here, whole blood plasma was collected from sheep and goat and purified by anion-exchange chromatography; the haemoglobins were crystallized by the hanging-drop vapour-diffusion method under unbuffered low-salt conditions using PEG 3350 as a precipitant. Data collection was carried out using a MAR345 image-plate detector system. Sheep haemoglobin crystallizes in the orthorhombic space group P2(1)2(1)2(1) with one whole biological molecule (alpha2beta2) in the asymmetric unit, with unit-cell parameters a = 60.231, b = 70.695, c = 131.479 A. In contrast, goat haemoglobin crystallizes in the triclinic system with two biological molecules (alpha2beta2) in the unit cell. The unit-cell parameters are a = 53.103, b = 69.382, c = 96.098 A, alpha = 110.867, beta = 91.133, gamma = 109.437 degrees.
Haemoglobin is a tetrameric protein that plays a vital role in the transport of oxygen from the lungs to the tissues and of carbon dioxide back to the lungs. Even though a large amount of work has already been performed in this area, the study of the haemoglobin structures of avian and mammalian species is rather incomplete. Efforts are being made to understand the salient features of the species mentioned above. Here, whole blood plasma was collected from sheep and goat and purified by anion-exchange chromatography; the haemoglobins were crystallized by the hanging-drop vapour-diffusion method under unbuffered low-salt conditions using PEG 3350 as a precipitant. Data collection was carried out using a MAR345 image-plate detector system. Sheep haemoglobin crystallizes in the orthorhombic space group P2(1)2(1)2(1) with one whole biological molecule (alpha2beta2) in the asymmetric unit, with unit-cell parameters a = 60.231, b = 70.695, c = 131.479 A. In contrast, goat haemoglobin crystallizes in the triclinic system with two biological molecules (alpha2beta2) in the unit cell. The unit-cell parameters are a = 53.103, b = 69.382, c = 96.098 A, alpha = 110.867, beta = 91.133, gamma = 109.437 degrees.


Crystallization of sheep (Ovis aries) and goat (Capra hircus) haemoglobins under unbuffered low-salt conditions.,Neelagandan K, Moorthy PS, Balasubramanian M, Ponnuswamy MN Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Oct 1;63(Pt, 10):887-9. Epub 2007 Sep 19. PMID:17909297<ref>PMID:17909297</ref>
Crystallization of sheep (Ovis aries) and goat (Capra hircus) haemoglobins under unbuffered low-salt conditions.,Neelagandan K, Moorthy PS, Balasubramanian M, Ponnuswamy MN Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Oct 1;63(Pt, 10):887-9. Epub 2007 Sep 19. PMID:017909297<ref>PMID:017909297</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</StructureSection>
</StructureSection>
[[Category: Capra hircus]]
[[Category: Capra hircus]]
[[Category: Balasubramanian, M]]
[[Category: Large Structures]]
[[Category: Moorthy, P Sathya]]
[[Category: Balasubramanian M]]
[[Category: Neelagandan, K]]
[[Category: Neelagandan K]]
[[Category: Ponnuswamy, M N]]
[[Category: Ponnuswamy MN]]
[[Category: Allosteric effect]]
[[Category: Sathya Moorthy P]]
[[Category: Heme]]
[[Category: Iron]]
[[Category: Low oxygen affinity]]
[[Category: Metal-binding]]
[[Category: Oxygen storage]]
[[Category: Oxygen transport]]
[[Category: Transport]]

Latest revision as of 09:04, 13 August 2026

Crystal Structure Determination of Goat Hemoglobin at 2.61 Angstrom Resolution

3d1a, resolution 2.61Å

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