1hmo
From Proteopedia
(New page: 200px<br /><applet load="1hmo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hmo, resolution 2.0Å" /> '''THE STRUCTURE OF DEOX...) |
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| - | [[Image:1hmo.jpg|left|200px]]<br /><applet load="1hmo" size=" | + | [[Image:1hmo.jpg|left|200px]]<br /><applet load="1hmo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hmo, resolution 2.0Å" /> | caption="1hmo, resolution 2.0Å" /> | ||
'''THE STRUCTURE OF DEOXY AND OXY HEMERYTHRIN AT 2.0 ANGSTROMS RESOLUTION'''<br /> | '''THE STRUCTURE OF DEOXY AND OXY HEMERYTHRIN AT 2.0 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystallographic structure analyses of deoxy and oxy hemerythrin have | + | The crystallographic structure analyses of deoxy and oxy hemerythrin have been carried out at 2.0 A resolution to extend the low resolution views of the physiological forms of this oxygen-binding protein. Restrained least-squares refinement has produced molecular models giving R-values of 16.8% for deoxy (41,064 reflections from 10 A to 2.0 A) and 17.3% for oxy hemerythrin (40,413 reflections from 10.0 A to 2.0 A). The protein structure in each derivative is very similar to that of myohemerythrin and the various met forms of hemerythrin. The binuclear complex in each derivative retains an oxygen atom bridging the two iron atoms, but the bond lengths found in deoxy hemerythrin support the idea that, in that form, the bridge is protonated, i.e. the bridging group is a hydroxyl. Dioxygen binds to the pentaco-ordinate iron atom in deoxy hemerythrin in the conversion to oxy hemerythrin. The interatomic distances are consistent with the proposed mechanism where the proton from the bridging group is transferred to the bound dioxygen, stabilizing it in the peroxo oxidation state by forming a hydrogen bond between the peroxy group and the bridging oxygen atom. |
==About this Structure== | ==About this Structure== | ||
| - | 1HMO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Themiste_dyscritum Themiste dyscritum] with ACE, FEO and OXY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1HMO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Themiste_dyscritum Themiste dyscritum] with <scene name='pdbligand=ACE:'>ACE</scene>, <scene name='pdbligand=FEO:'>FEO</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=1HMO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Themiste dyscritum]] | [[Category: Themiste dyscritum]] | ||
| - | [[Category: Holmes, M | + | [[Category: Holmes, M A.]] |
[[Category: Letrong, I.]] | [[Category: Letrong, I.]] | ||
| - | [[Category: Sieker, L | + | [[Category: Sieker, L C.]] |
| - | [[Category: Stenkamp, R | + | [[Category: Stenkamp, R E.]] |
[[Category: Turley, S.]] | [[Category: Turley, S.]] | ||
[[Category: ACE]] | [[Category: ACE]] | ||
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[[Category: oxygen transport]] | [[Category: oxygen transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:02:46 2008'' |
Revision as of 11:02, 21 February 2008
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THE STRUCTURE OF DEOXY AND OXY HEMERYTHRIN AT 2.0 ANGSTROMS RESOLUTION
Overview
The crystallographic structure analyses of deoxy and oxy hemerythrin have been carried out at 2.0 A resolution to extend the low resolution views of the physiological forms of this oxygen-binding protein. Restrained least-squares refinement has produced molecular models giving R-values of 16.8% for deoxy (41,064 reflections from 10 A to 2.0 A) and 17.3% for oxy hemerythrin (40,413 reflections from 10.0 A to 2.0 A). The protein structure in each derivative is very similar to that of myohemerythrin and the various met forms of hemerythrin. The binuclear complex in each derivative retains an oxygen atom bridging the two iron atoms, but the bond lengths found in deoxy hemerythrin support the idea that, in that form, the bridge is protonated, i.e. the bridging group is a hydroxyl. Dioxygen binds to the pentaco-ordinate iron atom in deoxy hemerythrin in the conversion to oxy hemerythrin. The interatomic distances are consistent with the proposed mechanism where the proton from the bridging group is transferred to the bound dioxygen, stabilizing it in the peroxo oxidation state by forming a hydrogen bond between the peroxy group and the bridging oxygen atom.
About this Structure
1HMO is a Single protein structure of sequence from Themiste dyscritum with , and as ligands. Full crystallographic information is available from OCA.
Reference
Structures of deoxy and oxy hemerythrin at 2.0 A resolution., Holmes MA, Le Trong I, Turley S, Sieker LC, Stenkamp RE, J Mol Biol. 1991 Apr 5;218(3):583-93. PMID:2016748
Page seeded by OCA on Thu Feb 21 13:02:46 2008
Categories: Single protein | Themiste dyscritum | Holmes, M A. | Letrong, I. | Sieker, L C. | Stenkamp, R E. | Turley, S. | ACE | FEO | OXY | Oxygen transport
