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1la6

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Revision as of 10:28, 20 March 2008 by OCA (Talk | contribs)
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PDB ID 1la6

Drag the structure with the mouse to rotate
, resolution 2.0Å
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



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

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