1faw: Difference between revisions
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[[Image: | ==GRAYLAG GOOSE HEMOGLOBIN (OXY FORM)== | ||
<StructureSection load='1faw' size='340' side='right' caption='[[1faw]], [[Resolution|resolution]] 3.09Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1faw]] is a 4 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FAW FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene><br> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1faw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1faw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1faw RCSB], [http://www.ebi.ac.uk/pdbsum/1faw PDBsum]</span></td></tr> | |||
<table> | |||
== 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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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:11717498<ref>PMID:11717498</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Hemoglobin|Hemoglobin]] | *[[Hemoglobin 3D structures|Hemoglobin 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Anser anser]] | [[Category: Anser anser]] | ||
[[Category: Liang, Y H.]] | [[Category: Liang, Y H.]] | ||
Revision as of 14:59, 28 September 2014
GRAYLAG GOOSE HEMOGLOBIN (OXY FORM)GRAYLAG GOOSE HEMOGLOBIN (OXY FORM)
Structural highlights
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 PubMedThe 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. 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:11717498[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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