1s5y
From Proteopedia
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| - | [[Image:1s5y.jpg|left|200px]] | + | [[Image:1s5y.jpg|left|200px]] |
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| - | '''The crystal structure of Trematomus bernacchii hemoglobin oxidized by ferricyanide''' | + | {{Structure |
| + | |PDB= 1s5y |SIZE=350|CAPTION= <scene name='initialview01'>1s5y</scene>, resolution 2.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> and <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''The crystal structure of Trematomus bernacchii hemoglobin oxidized by ferricyanide''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1S5Y is a [ | + | 1S5Y is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Trematomus_bernacchii Trematomus bernacchii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S5Y OCA]. |
==Reference== | ==Reference== | ||
| - | The oxidation process of Antarctic fish hemoglobins., Vitagliano L, Bonomi G, Riccio A, di Prisco G, Smulevich G, Mazzarella L, Eur J Biochem. 2004 May;271(9):1651-9. PMID:[http:// | + | The oxidation process of Antarctic fish hemoglobins., Vitagliano L, Bonomi G, Riccio A, di Prisco G, Smulevich G, Mazzarella L, Eur J Biochem. 2004 May;271(9):1651-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15096204 15096204] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Trematomus bernacchii]] | [[Category: Trematomus bernacchii]] | ||
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[[Category: oxidation]] | [[Category: oxidation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:00:55 2008'' |
Revision as of 12:00, 20 March 2008
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| , resolution 2.50Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
The crystal structure of Trematomus bernacchii hemoglobin oxidized by ferricyanide
Overview
Analysis of the molecular properties of proteins extracted from organisms living under extreme conditions often highlights peculiar features. We investigated by UV-visible spectroscopy and X-ray crystallography the oxidation process, promoted by air or ferricyanide, of five hemoglobins extracted from Antarctic fishes (Notothenioidei). Spectroscopic analysis revealed that these hemoglobins share a common oxidation pathway, which shows striking differences from the oxidation processes of hemoglobins from other vertebrates. Indeed, simple exposure of these hemoglobins to air leads to the formation of a significant amount of the low-spin hexacoordinated form, denoted hemichrome. This hemichrome form, which is detected under a variety of experimental conditions, can be reversibly transformed to either carbomonoxy or deoxygenated forms with reducing agents. Interestingly, the spectra of the fully oxidized species, obtained by treating the protein with ferricyanide, show the simultaneous presence of peaks corresponding to different hexacoordinated states, the aquomet and the hemichrome. In order to assign the heme region state of the alpha and beta chains, the air-oxidized and ferricyanide-oxidized forms of Trematomus bernacchii hemoglobin were crystallized. Crystallographic analysis revealed that these forms correspond to an alpha(aquomet)-beta(bishistidyl-hemichrome) state. This demonstrates that the alpha and beta chains of Antarctic fish hemoglobins follow very different oxidation pathways. As found for Trematomus newnesi hemoglobin in a partial hemichrome state [Riccio, A., Vitagliano, L., di Prisco, G., Zagari, A. & Mazzarella, L. (2002) Proc. Natl Acad. Sci. USA99, 9801-9806], the quaternary structures of these alpha(aquomet)-beta(bishistidyl-hemichrome) forms are intermediate between the physiological R and T hemoglobin states. Together, these structures provide information on the general features of this intermediate state.
About this Structure
1S5Y is a Protein complex structure of sequences from Trematomus bernacchii. Full crystallographic information is available from OCA.
Reference
The oxidation process of Antarctic fish hemoglobins., Vitagliano L, Bonomi G, Riccio A, di Prisco G, Smulevich G, Mazzarella L, Eur J Biochem. 2004 May;271(9):1651-9. PMID:15096204
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