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1spg

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{{STRUCTURE_1spg| PDB=1spg | SCENE= }}
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'''CARBONMONOXY HEMOGLOBIN FROM THE TELEOST FISH LEIOSTOMUS XANTHURUS'''
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===CARBONMONOXY HEMOGLOBIN FROM THE TELEOST FISH LEIOSTOMUS XANTHURUS===
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==Overview==
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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--&gt;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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8605630 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8605630}}
==About this Structure==
==About this Structure==
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[[Category: Root effect]]
[[Category: Root effect]]
[[Category: Teleost fish]]
[[Category: Teleost fish]]
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Revision as of 16:03, 28 July 2008

Image:1spg.png

Template:STRUCTURE 1spg

CARBONMONOXY HEMOGLOBIN FROM THE TELEOST FISH LEIOSTOMUS XANTHURUS

Template:ABSTRACT PUBMED 8605630

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

Page seeded by OCA on Mon Jul 28 19:03:04 2008

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