1hbi: Difference between revisions

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New page: left|200px<br /> <applet load="1hbi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hbi, resolution 1.7Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1hbi.gif|left|200px]]<br />
[[Image:1hbi.gif|left|200px]]<br /><applet load="1hbi" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1hbi" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1hbi, resolution 1.7&Aring;" />
caption="1hbi, resolution 1.7&Aring;" />
'''CRYSTAL STRUCTURE OF OXYGENATED SCAPHARCA DIMERIC HEMOGLOBIN AT 1.7 ANGSTROMS RESOLUTION'''<br />
'''CRYSTAL STRUCTURE OF OXYGENATED SCAPHARCA DIMERIC HEMOGLOBIN AT 1.7 ANGSTROMS RESOLUTION'''<br />


==Overview==
==Overview==
The crystal structure of the cooperative dimeric hemoglobin from the blood, clam Scapharca inaequivalvis has been determined in the oxygenated state, and refined to an R-factor of 0.157 at 1.7-A resolution. The structure is, very similar to the carbon monoxide-liganded form with subtle differences, in ligand binding geometry. Oxygen binds to the heme iron in a bent, conformation with Fe-O-O angles of 135 degrees and 150 degrees for the two, subunits. These observed angles are lower than the equivalent angles in, the carbon monoxide-liganded form and intermediate between the angles, observed in structures of oxygenated sperm whale myoglobin and oxygenated, human hemoglobin. This third high resolution structure of Scapharca, dimeric hemoglobin permits a detailed analysis of the water structure in, the highly hydrated interface between subunits.
The crystal structure of the cooperative dimeric hemoglobin from the blood clam Scapharca inaequivalvis has been determined in the oxygenated state and refined to an R-factor of 0.157 at 1.7-A resolution. The structure is very similar to the carbon monoxide-liganded form with subtle differences in ligand binding geometry. Oxygen binds to the heme iron in a bent conformation with Fe-O-O angles of 135 degrees and 150 degrees for the two subunits. These observed angles are lower than the equivalent angles in the carbon monoxide-liganded form and intermediate between the angles observed in structures of oxygenated sperm whale myoglobin and oxygenated human hemoglobin. This third high resolution structure of Scapharca dimeric hemoglobin permits a detailed analysis of the water structure in the highly hydrated interface between subunits.


==About this Structure==
==About this Structure==
1HBI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Scapharca_inaequivalvis Scapharca inaequivalvis] with HEM and OXY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HBI OCA].  
1HBI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Scapharca_inaequivalvis Scapharca inaequivalvis] 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=1HBI OCA].  


==Reference==
==Reference==
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[[Category: Scapharca inaequivalvis]]
[[Category: Scapharca inaequivalvis]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Condon, P.J.]]
[[Category: Condon, P J.]]
[[Category: Junior, W.E.Royer.]]
[[Category: Junior, W E.Royer.]]
[[Category: HEM]]
[[Category: HEM]]
[[Category: OXY]]
[[Category: OXY]]
[[Category: oxygen transport]]
[[Category: oxygen transport]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:59:29 2008''

Revision as of 13:59, 21 February 2008

File:1hbi.gif


1hbi, resolution 1.7Å

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CRYSTAL STRUCTURE OF OXYGENATED SCAPHARCA DIMERIC HEMOGLOBIN AT 1.7 ANGSTROMS RESOLUTION

OverviewOverview

The crystal structure of the cooperative dimeric hemoglobin from the blood clam Scapharca inaequivalvis has been determined in the oxygenated state and refined to an R-factor of 0.157 at 1.7-A resolution. The structure is very similar to the carbon monoxide-liganded form with subtle differences in ligand binding geometry. Oxygen binds to the heme iron in a bent conformation with Fe-O-O angles of 135 degrees and 150 degrees for the two subunits. These observed angles are lower than the equivalent angles in the carbon monoxide-liganded form and intermediate between the angles observed in structures of oxygenated sperm whale myoglobin and oxygenated human hemoglobin. This third high resolution structure of Scapharca dimeric hemoglobin permits a detailed analysis of the water structure in the highly hydrated interface between subunits.

About this StructureAbout this Structure

1HBI is a Single protein structure of sequence from Scapharca inaequivalvis with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of oxygenated Scapharca dimeric hemoglobin at 1.7-A resolution., Condon PJ, Royer WE Jr, J Biol Chem. 1994 Oct 14;269(41):25259-67. PMID:7929217

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