1la6
From Proteopedia
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|PDB= 1la6 |SIZE=350|CAPTION= <scene name='initialview01'>1la6</scene>, resolution 2.0Å | |PDB= 1la6 |SIZE=350|CAPTION= <scene name='initialview01'>1la6</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1t1n|1T1N]] | ||
| + | |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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[[Category: Vitagliano, L.]] | [[Category: Vitagliano, L.]] | ||
[[Category: Zagari, A.]] | [[Category: Zagari, A.]] | ||
| - | [[Category: ACE]] | ||
| - | [[Category: CMO]] | ||
| - | [[Category: HEM]] | ||
[[Category: bishistidine complex]] | [[Category: bishistidine complex]] | ||
[[Category: hemichrome]] | [[Category: hemichrome]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:00:14 2008'' |
Revision as of 19:00, 30 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1T1N
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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