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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1a4f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Anser_indicus Anser indicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A4F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A4F FirstGlance]. <br>
<table><tr><td colspan='2'>[[1a4f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Anser_indicus Anser indicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A4F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A4F 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>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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&#8491;</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>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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=1a4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a4f OCA], [https://pdbe.org/1a4f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a4f RCSB], [https://www.ebi.ac.uk/pdbsum/1a4f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a4f 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=1a4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a4f OCA], [https://pdbe.org/1a4f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a4f RCSB], [https://www.ebi.ac.uk/pdbsum/1a4f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a4f ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/HBA_ANSIN HBA_ANSIN]] Involved in oxygen transport from the lung to the various peripheral tissues. [[https://www.uniprot.org/uniprot/HBB_ANSIN HBB_ANSIN]] Involved in oxygen transport from the lung to the various peripheral tissues.  
[https://www.uniprot.org/uniprot/HBA_ANSIN HBA_ANSIN] 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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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a4f ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a4f ConSurf].
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== Publication Abstract from PubMed ==
We have determined the crystal structure of bar-headed goose haemoglobin in the oxy form to a resolution of 2.0 A. The R-factor of the model is 19.8%. The structure is similar to human HbA, but contacts between the subunits show slightly altered packing of the tetramer. Bar-headed goose blood shows a greatly elevated oxygen affinity compared to closely related species of geese. This is apparently due to a single proline to alanine mutation at the alpha 1 beta 1 interface which destabilises the T state of the protein. The beta chain N and C termini are well-localized, and together with other neighbouring basic groups they form a strongly positively charged groove at the entrance to the central cavity around the molecular dyad. The well-ordered conformation and the three-dimensional distribution of positive charges clearly indicate this area to be the inositol pentaphosphate binding site of bird haemoglobins.
The crystal structure of a high oxygen affinity species of haemoglobin (bar-headed goose haemoglobin in the oxy form).,Zhang J, Hua Z, Tame JR, Lu G, Zhang R, Gu X J Mol Biol. 1996 Jan 26;255(3):484-93. PMID:8568892<ref>PMID:8568892</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1a4f" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Anser indicus]]
[[Category: Anser indicus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Gu, X]]
[[Category: Gu X]]
[[Category: Zhang, J]]
[[Category: Zhang J]]
[[Category: Erythrocyte]]
[[Category: Heme]]
[[Category: Oxygen transport]]
[[Category: Respiratory protein]]

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