1spg
From Proteopedia
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|PDB= 1spg |SIZE=350|CAPTION= <scene name='initialview01'>1spg</scene>, resolution 1.95Å | |PDB= 1spg |SIZE=350|CAPTION= <scene name='initialview01'>1spg</scene>, resolution 1.95Å | ||
|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= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1spg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1spg OCA], [http://www.ebi.ac.uk/pdbsum/1spg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1spg RCSB]</span> | ||
}} | }} | ||
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[[Category: Getzoff, E D.]] | [[Category: Getzoff, E D.]] | ||
[[Category: Mylvaganam, S E.]] | [[Category: Mylvaganam, S E.]] | ||
| - | [[Category: ACE]] | ||
| - | [[Category: CMO]] | ||
| - | [[Category: HEM]] | ||
[[Category: carbon monoxide]] | [[Category: carbon monoxide]] | ||
[[Category: globin]] | [[Category: globin]] | ||
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[[Category: teleost fish]] | [[Category: teleost fish]] | ||
| - | ''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 23:45:15 2008'' |
Revision as of 20:45, 30 March 2008
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| , resolution 1.95Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CARBONMONOXY HEMOGLOBIN FROM THE TELEOST FISH LEIOSTOMUS XANTHURUS
Overview
The remarkable ability of root effect haemoglobins to pump oxygen against high O2 gradients results from extreme, acid-induced reductions in O2 affinity and cooperativity. The long-sought mechanism for the root effect, revealed by the 2 angstrom crystal structure of the ligand-bound haemoglobin from Leiostomus xanthurus at pH 7.5, unexpectedly involves modulation of the R-state. Key residues strategically assemble positive-charge clusters across the allosteric beta1 beta2-interface in the R-state. At low pH, protonation of the beta N terminus and His 147(HC3)beta within these clusters is postulated to destabilize the R-state and promote the acid-triggered, allosteric R-->T switch with concomitant O2 release. Surprisingly, a set of residues specific to root effect haemoglobins recruit additional residues, conserved among most haemoglobins, to produce the root effect.
About this Structure
1SPG is a Protein complex structure of sequences from Leiostomus xanthurus. Full crystallographic information is available from OCA.
Reference
Structural basis for the root effect in haemoglobin., Mylvaganam SE, Bonaventura C, Bonaventura J, Getzoff ED, Nat Struct Biol. 1996 Mar;3(3):275-83. PMID:8605630
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