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1ash

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[[Image:1ash.gif|left|200px]]<br /><applet load="1ash" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ash.gif|left|200px]]
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caption="1ash, resolution 2.15&Aring;" />
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'''THE STRUCTURE OF ASCARIS HEMOGLOBIN DOMAIN I AT 2.2 ANGSTROMS RESOLUTION: MOLECULAR FEATURES OF OXYGEN AVIDITY'''<br />
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{{Structure
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|PDB= 1ash |SIZE=350|CAPTION= <scene name='initialview01'>1ash</scene>, resolution 2.15&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=OXY:OXYGEN MOLECULE'>OXY</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''THE STRUCTURE OF ASCARIS HEMOGLOBIN DOMAIN I AT 2.2 ANGSTROMS RESOLUTION: MOLECULAR FEATURES OF OXYGEN AVIDITY'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1ASH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum] 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=1ASH OCA].
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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].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=7753786 7753786]
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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: Single protein]]
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[[Category: oxygen storage]]
[[Category: oxygen storage]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:47:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:01:43 2008''

Revision as of 08:01, 20 March 2008

Image:1ash.gif


PDB ID 1ash

Drag the structure with the mouse to rotate
, resolution 2.15Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



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


Overview

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.

About this Structure

1ASH is a Single protein structure of sequence from Ascaris suum. Full crystallographic information is available from OCA.

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:7753786

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