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[[Image:1ash.gif|left|200px]]


{{Structure
==THE STRUCTURE OF ASCARIS HEMOGLOBIN DOMAIN I AT 2.2 ANGSTROMS RESOLUTION: MOLECULAR FEATURES OF OXYGEN AVIDITY==
|PDB= 1ash |SIZE=350|CAPTION= <scene name='initialview01'>1ash</scene>, resolution 2.15&Aring;
<StructureSection load='1ash' size='340' side='right'caption='[[1ash]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=OXY:OXYGEN MOLECULE'>OXY</scene>
<table><tr><td colspan='2'>[[1ash]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ASH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ASH FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
|GENE=  
<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=1ash FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ash OCA], [https://pdbe.org/1ash PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ash RCSB], [https://www.ebi.ac.uk/pdbsum/1ash PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ash ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GLB_ASCSU GLB_ASCSU] Has an extremely high oxygen affinity. In a vacuum, it takes several minutes to release its oxygen compared to milliseconds for a normal globin. Could be used as an oxygen scavenger for sterol biosynthesis.
== 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/as/1ash_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ash ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The perienteric hemoglobin of the parasitic nematode Ascaris has an exceptionally high affinity for oxygen. It is an octameric protein containing two similar heme-binding domains per subunit, but recombinant constructs expressing a single, monomeric heme-binding domain (domain 1; D1) retain full oxygen avidity. We have solved the crystal structure of D1 at 2.2 A resolution. Analysis of the structure reveals a characteristic globin fold and illuminates molecular features involved in oxygen avidity of Ascaris perienteric hemoglobin. A strong hydrogen bond between tyrosine at position 10 in the B helix (tyrosine-B10) and the distal oxygen of the ligand, combined with a weak hydrogen bond between glutamine-E7 and the proximal oxygen, grips the ligand in the binding pocket. A third hydrogen bond between these two amino acids appears to stabilize the structure. The B helix of D1 is displaced laterally by 2.5 A when compared with sperm whale myoglobin. This shifts the tyrosine-B10 hydroxyl far enough from liganded oxygen to form a strong hydrogen bond without steric hindrance. Changes in the F helix compared with myoglobin contribute to a tilted heme that may also be important for oxygen affinity.


'''THE STRUCTURE OF ASCARIS HEMOGLOBIN DOMAIN I AT 2.2 ANGSTROMS RESOLUTION: MOLECULAR FEATURES OF OXYGEN AVIDITY'''
The structure of Ascaris hemoglobin domain I at 2.2 A resolution: molecular features of oxygen avidity.,Yang J, Kloek AP, Goldberg DE, Mathews FS Proc Natl Acad Sci U S A. 1995 May 9;92(10):4224-8. PMID:7753786<ref>PMID:7753786</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ash" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
The perienteric hemoglobin of the parasitic nematode Ascaris has an exceptionally high affinity for oxygen. It is an octameric protein containing two similar heme-binding domains per subunit, but recombinant constructs expressing a single, monomeric heme-binding domain (domain 1; D1) retain full oxygen avidity. We have solved the crystal structure of D1 at 2.2 A resolution. Analysis of the structure reveals a characteristic globin fold and illuminates molecular features involved in oxygen avidity of Ascaris perienteric hemoglobin. A strong hydrogen bond between tyrosine at position 10 in the B helix (tyrosine-B10) and the distal oxygen of the ligand, combined with a weak hydrogen bond between glutamine-E7 and the proximal oxygen, grips the ligand in the binding pocket. A third hydrogen bond between these two amino acids appears to stabilize the structure. The B helix of D1 is displaced laterally by 2.5 A when compared with sperm whale myoglobin. This shifts the tyrosine-B10 hydroxyl far enough from liganded oxygen to form a strong hydrogen bond without steric hindrance. Changes in the F helix compared with myoglobin contribute to a tilted heme that may also be important for oxygen affinity.
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
 
== References ==
==About this Structure==
<references/>
1ASH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ASH OCA].
__TOC__
 
</StructureSection>
==Reference==
The structure of Ascaris hemoglobin domain I at 2.2 A resolution: molecular features of oxygen avidity., Yang J, Kloek AP, Goldberg DE, Mathews FS, Proc Natl Acad Sci U S A. 1995 May 9;92(10):4224-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7753786 7753786]
[[Category: Ascaris suum]]
[[Category: Ascaris suum]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Goldberg, D E.]]
[[Category: Goldberg DE]]
[[Category: Kloek, A P.]]
[[Category: Kloek AP]]
[[Category: Mathews, F S.]]
[[Category: Mathews FS]]
[[Category: Yang, J.]]
[[Category: Yang J]]
[[Category: HEM]]
[[Category: OXY]]
[[Category: oxygen storage]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:01:43 2008''

Latest revision as of 05:24, 13 August 2026

THE STRUCTURE OF ASCARIS HEMOGLOBIN DOMAIN I AT 2.2 ANGSTROMS RESOLUTION: MOLECULAR FEATURES OF OXYGEN AVIDITY

1ash, resolution 2.15Å

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