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New page: left|200px<br /> <applet load="1c40" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c40, resolution 2.30Å" /> '''BAR-HEADED GOOSE HE... |
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== | ==BAR-HEADED GOOSE HEMOGLOBIN (AQUOMET FORM)== | ||
Haemoglobin from the bar-headed goose (Anser indicus) has higher oxygen | <StructureSection load='1c40' size='340' side='right'caption='[[1c40]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1c40]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Anser_indicus Anser indicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1c0h 1c0h]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C40 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C40 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</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=1c40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c40 OCA], [https://pdbe.org/1c40 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c40 RCSB], [https://www.ebi.ac.uk/pdbsum/1c40 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c40 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/HBA_ANSIN HBA_ANSIN] Involved in oxygen transport from the lung to the various peripheral tissues. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c4/1c40_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1c40 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Haemoglobin from the bar-headed goose (Anser indicus) has higher oxygen affinity than that from its lowland relatives such as greylag goose (A. anser). The crystal structure of bar-headed goose aquomet haemoglobin was determined at 2.3 A resolution and compared with the structures of the goose oxy, human, horse and other avian haemoglobins and the sequences of other avian haemoglobins. Four amino-acid residues differ between greylag goose and bar-headed goose haemoglobins, among which Alaalpha119 and Aspbeta125 in bar-headed goose haemoglobin reduces the contacts between the alpha(1) and beta(1) subunits compared with Pro and Glu, respectively, and therefore may increase the oxygen affinity by loosening the alpha(1)beta(1) interface. Compared with human oxy haemoglobin, the relative orientation of two alphabeta dimers in the bar-headed goose aquomet and oxy Hbs are rotated by about 4 degrees, indicating a unique quaternary structural difference from the typical R state. This new 'R(H)' state is probably correlated with the higher oxygen affinity of bar-headed goose haemoglobin. | |||
Avian haemoglobins and structural basis of high affinity for oxygen: structure of bar-headed goose aquomet haemoglobin.,Liu XZ, Li SL, Jing H, Liang YH, Hua ZQ, Lu GY Acta Crystallogr D Biol Crystallogr. 2001 Jun;57(Pt 6):775-83. Epub 2001, May 25. PMID:11375496<ref>PMID:11375496</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1c40" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Anser indicus]] | [[Category: Anser indicus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Hua | [[Category: Hua Z]] | ||
[[Category: Jing | [[Category: Jing H]] | ||
[[Category: Li | [[Category: Li S]] | ||
[[Category: Liu | [[Category: Liu X]] | ||
[[Category: Lu | [[Category: Lu G]] | ||
[[Category: Zhang | [[Category: Zhang R]] | ||
Latest revision as of 08:47, 9 August 2023
BAR-HEADED GOOSE HEMOGLOBIN (AQUOMET FORM)BAR-HEADED GOOSE HEMOGLOBIN (AQUOMET FORM)
Structural highlights
FunctionHBA_ANSIN 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 PubMedHaemoglobin from the bar-headed goose (Anser indicus) has higher oxygen affinity than that from its lowland relatives such as greylag goose (A. anser). The crystal structure of bar-headed goose aquomet haemoglobin was determined at 2.3 A resolution and compared with the structures of the goose oxy, human, horse and other avian haemoglobins and the sequences of other avian haemoglobins. Four amino-acid residues differ between greylag goose and bar-headed goose haemoglobins, among which Alaalpha119 and Aspbeta125 in bar-headed goose haemoglobin reduces the contacts between the alpha(1) and beta(1) subunits compared with Pro and Glu, respectively, and therefore may increase the oxygen affinity by loosening the alpha(1)beta(1) interface. Compared with human oxy haemoglobin, the relative orientation of two alphabeta dimers in the bar-headed goose aquomet and oxy Hbs are rotated by about 4 degrees, indicating a unique quaternary structural difference from the typical R state. This new 'R(H)' state is probably correlated with the higher oxygen affinity of bar-headed goose haemoglobin. Avian haemoglobins and structural basis of high affinity for oxygen: structure of bar-headed goose aquomet haemoglobin.,Liu XZ, Li SL, Jing H, Liang YH, Hua ZQ, Lu GY Acta Crystallogr D Biol Crystallogr. 2001 Jun;57(Pt 6):775-83. Epub 2001, May 25. PMID:11375496[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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