1la6: Difference between revisions

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[[Image:1la6.gif|left|200px]]
{{Seed}}
[[Image:1la6.png|left|200px]]


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{{STRUCTURE_1la6|  PDB=1la6  |  SCENE=  }}  
{{STRUCTURE_1la6|  PDB=1la6  |  SCENE=  }}  


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




==Overview==
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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 --&gt; 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 --&gt; T transition of tetrameric hemoglobins.
The line below this paragraph, {{ABSTRACT_PUBMED_12093902}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_12093902}}


==About this Structure==
==About this Structure==
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[[Category: Bishistidine complex]]
[[Category: Bishistidine complex]]
[[Category: Hemichrome]]
[[Category: Hemichrome]]
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