1hmo

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[[Image:1hmo.jpg|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1hmo", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hmo OCA], [http://www.ebi.ac.uk/pdbsum/1hmo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hmo RCSB]</span>
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'''THE STRUCTURE OF DEOXY AND OXY HEMERYTHRIN AT 2.0 ANGSTROMS RESOLUTION'''
'''THE STRUCTURE OF DEOXY AND OXY HEMERYTHRIN AT 2.0 ANGSTROMS RESOLUTION'''
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[[Category: Stenkamp, R E.]]
[[Category: Stenkamp, R E.]]
[[Category: Turley, S.]]
[[Category: Turley, S.]]
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[[Category: oxygen transport]]
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[[Category: Oxygen transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:01:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:07:42 2008''
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Revision as of 16:01, 2 May 2008

Image:1hmo.jpg

Template:STRUCTURE 1hmo

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. 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 Fri May 2 19:01:06 2008

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