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[[Image:1faw.jpg|left|200px]]<br /><applet load="1faw" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1faw, resolution 3.09&Aring;" />
'''GRAYLAG GOOSE HEMOGLOBIN (OXY FORM)'''<br />


==Overview==
==GRAYLAG GOOSE HEMOGLOBIN (OXY FORM)==
The greylag goose (Anser anser), which lives on lowlands and cannot, tolerate hypoxic conditions, presents a striking contrast to its close, relative the bar-headed goose (A. indicus), which lives at high altitude, and possesses high-altitude hypoxia adaptation. There are only four, amino-acid residue differences at alpha18, alpha63, alpha119 and beta125, between the haemoglobins of the two species. The crystal structure of, greylag goose oxy haemoglobin was determined at 3.09 A resolution. Its, quaternary structure is slightly different from that of the bar-headed, goose oxy haemoglobin, with a rotation of 2.8 degrees in relative, orientation of the two dimers. Of the four mutations, those at alpha119, and beta125 produce contact changes in the alpha(1)beta(1) interface and, may be responsible for the differences in intrinsic oxygen affinity, between the two species; those at alpha18 and alpha63 may be responsible, for the differences in quaternary structure between the two species.
<StructureSection load='1faw' size='340' side='right'caption='[[1faw]], [[Resolution|resolution]] 3.09&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1faw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Anser_anser Anser anser]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FAW 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]] 3.09&#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=1faw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1faw OCA], [https://pdbe.org/1faw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1faw RCSB], [https://www.ebi.ac.uk/pdbsum/1faw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1faw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HBA_ANSAN HBA_ANSAN] 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/fa/1faw_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=1faw ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1FAW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Anser_anser Anser anser] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=OXY:'>OXY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FAW OCA].
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
The structure of greylag goose oxy haemoglobin: the roles of four mutations compared with bar-headed goose haemoglobin., Liang YH, Liu XZ, Liu SH, Lu GY, Acta Crystallogr D Biol Crystallogr. 2001 Dec;57(Pt 12):1850-6. Epub 2001, Nov 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11717498 11717498]
[[Category: Anser anser]]
[[Category: Anser anser]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Liang, Y.H.]]
[[Category: Liang Y-H]]
[[Category: Liu, S.H.]]
[[Category: Liu S-H]]
[[Category: Liu, X.Z.]]
[[Category: Liu X-Z]]
[[Category: Lu, G.Y.]]
[[Category: Lu G-Y]]
[[Category: HEM]]
[[Category: OXY]]
[[Category: erythrocyte]]
[[Category: heme]]
[[Category: oxygen transport]]
[[Category: respiratory protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:46:43 2008''

Latest revision as of 10:12, 7 February 2024

GRAYLAG GOOSE HEMOGLOBIN (OXY FORM)GRAYLAG GOOSE HEMOGLOBIN (OXY FORM)

Structural highlights

1faw is a 4 chain structure with sequence from Anser anser. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.09Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HBA_ANSAN 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.

See Also

1faw, resolution 3.09Å

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