1pbx: Difference between revisions

Revision as of 15:27, 21 February 2008

HAEMOGLOBIN OF THE ANTARCTIC FISH PAGOTHENIA BERNACCHII: AMINO ACID SEQUENCE, OXYGEN EQUILIBRIA AND CRYSTAL STRUCTURE OF ITS CARBONMONOXY DERIVATIVE

OverviewOverview

The Antarctic fish Pagothenia bernacchii has one major haemoglobin, Hb1 (over 95% of the total blood content). Hb1 has a strong alkaline Bohr effect and at low pH exhibits the reduced ligand affinity and co-operativity that comprise the Root effect. We have determined the complete amino acid sequence of P. bernacchii Hb1 and also the structure of its carbonmonoxy derivative by X-ray crystallography, to a resolution of 2.5 A. The crystallographic R-factor of the refined structure is 18%. The three-dimensional structure of this fish haemoglobin is similar to that of human haemoglobin A, with a root-mean-square difference in main-chain atom positions of 1.4 A after superimposition of the two structures, despite only 48% homology of their amino acid sequences (including insertion of a single residue in the CD region of the fish alpha-chain). Large structural differences occur only at the N and C termini of both the alpha- and beta-chains. Neither these nor other smaller structural differences provide any obvious explanation of the Root effect of this or other fish haemoglobins.

About this StructureAbout this Structure

1PBX is a Protein complex structure of sequences from Trematomus bernacchii with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Haemoglobin of the antarctic fish Pagothenia bernacchii. Amino acid sequence, oxygen equilibria and crystal structure of its carbonmonoxy derivative., Camardella L, Caruso C, D'Avino R, di Prisco G, Rutigliano B, Tamburrini M, Fermi G, Perutz MF, J Mol Biol. 1992 Mar 20;224(2):449-60. PMID:1560461

Page seeded by OCA on Thu Feb 21 14:27:13 2008

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OCA

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-[[Image:1pbx.gif|left|200px]]<br />
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 '''HAEMOGLOBIN OF THE ANTARCTIC FISH PAGOTHENIA BERNACCHII: AMINO ACID SEQUENCE, OXYGEN EQUILIBRIA AND CRYSTAL STRUCTURE OF ITS CARBONMONOXY DERIVATIVE'''<br />
 ==Overview==
-The Antarctic fish Pagothenia bernacchii has one major haemoglobin, Hb1, (over 95% of the total blood content). Hb1 has a strong alkaline Bohr, effect and at low pH exhibits the reduced ligand affinity and, co-operativity that comprise the Root effect. We have determined the, complete amino acid sequence of P. bernacchii Hb1 and also the structure, of its carbonmonoxy derivative by X-ray crystallography, to a resolution, of 2.5 A. The crystallographic R-factor of the refined structure is 18%., The three-dimensional structure of this fish haemoglobin is similar to, that of human haemoglobin A, with a root-mean-square difference in, main-chain atom positions of 1.4 A after superimposition of the two, structures, despite only 48% homology of their amino acid sequences, (including insertion of a single residue in the CD region of the fish, alpha-chain). Large structural differences occur only at the N and C, termini of both the alpha- and beta-chains. Neither these nor other, smaller structural differences provide any obvious explanation of the Root, effect of this or other fish haemoglobins.
+The Antarctic fish Pagothenia bernacchii has one major haemoglobin, Hb1 (over 95% of the total blood content). Hb1 has a strong alkaline Bohr effect and at low pH exhibits the reduced ligand affinity and co-operativity that comprise the Root effect. We have determined the complete amino acid sequence of P. bernacchii Hb1 and also the structure of its carbonmonoxy derivative by X-ray crystallography, to a resolution of 2.5 A. The crystallographic R-factor of the refined structure is 18%. The three-dimensional structure of this fish haemoglobin is similar to that of human haemoglobin A, with a root-mean-square difference in main-chain atom positions of 1.4 A after superimposition of the two structures, despite only 48% homology of their amino acid sequences (including insertion of a single residue in the CD region of the fish alpha-chain). Large structural differences occur only at the N and C termini of both the alpha- and beta-chains. Neither these nor other smaller structural differences provide any obvious explanation of the Root effect of this or other fish haemoglobins.
 ==About this Structure==
-PBX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Trematomus_bernacchii Trematomus bernacchii] with HEM and CMO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PBX OCA].
+PBX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Trematomus_bernacchii Trematomus bernacchii] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=CMO:'>CMO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PBX OCA].
 ==Reference==
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 [[Category: oxygen transport]]
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