1la6

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[[Image:1la6.gif|left|200px]]
[[Image:1la6.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1la6", creates the "Structure Box" on the page.
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{{STRUCTURE_1la6| PDB=1la6 | SCENE= }}
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|RELATEDENTRY=[[1t1n|1T1N]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1la6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1la6 OCA], [http://www.ebi.ac.uk/pdbsum/1la6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1la6 RCSB]</span>
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'''The crystal structure of Trematomus newnesi hemoglobin in a partial hemichrome state'''
'''The crystal structure of Trematomus newnesi hemoglobin in a partial hemichrome state'''
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[[Category: Vitagliano, L.]]
[[Category: Vitagliano, L.]]
[[Category: Zagari, A.]]
[[Category: Zagari, A.]]
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[[Category: bishistidine complex]]
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[[Category: Bishistidine complex]]
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[[Category: hemichrome]]
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[[Category: Hemichrome]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:43:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:00:14 2008''
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Revision as of 20:43, 2 May 2008

Image:1la6.gif

Template:STRUCTURE 1la6

The crystal structure of Trematomus newnesi hemoglobin in a partial hemichrome state


Overview

Tetrameric hemoglobins are the most widely used systems in studying protein cooperativity. Allosteric effects in hemoglobins arise from the switch between a relaxed (R) state and a tense (T) state occurring upon oxygen release. Here we report the 2.0-A crystal structure of the main hemoglobin component of the Antarctic fish Trematomus newnesi, in a partial hemichrome form. The two alpha-subunit iron atoms are bound to a CO molecule, whereas in the beta subunits the distal histidine residue is the sixth ligand of the heme iron. This structure, a tetrameric hemoglobin in the hemichrome state, demonstrates that the iron coordination by the distal histidine, usually associated with denaturing states, may be tolerated in a native-like hemoglobin structure. In addition, several features of the tertiary and quaternary organization of this structure are intermediate between the R and T states and agree well with the R --> T transition state properties obtained by spectroscopic and kinetic techniques. The analysis of this structure provides a detailed pathway of heme-heme communication and it indicates that the plasticity of the beta heme pocket plays a role in the R --> T transition of tetrameric hemoglobins.

About this Structure

1LA6 is a Protein complex structure of sequences from Trematomus newnesi. Full crystallographic information is available from OCA.

Reference

The crystal structure of a tetrameric hemoglobin in a partial hemichrome state., Riccio A, Vitagliano L, di Prisco G, Zagari A, Mazzarella L, Proc Natl Acad Sci U S A. 2002 Jul 23;99(15):9801-6. Epub 2002 Jul 1. PMID:12093902 Page seeded by OCA on Fri May 2 23:43:07 2008

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