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PDBsum entry 1coh
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Oxygen transport
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PDB id
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1coh
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure of haemoglobin in the deoxy quaternary state with ligand bound at the alpha haems.
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Authors
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B.Luisi,
N.Shibayama.
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Ref.
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J Mol Biol, 1989,
206,
723-736.
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PubMed id
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Abstract
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We report the X-ray crystal structure of two analogues of human haemoglobin in
the deoxy quaternary (T) state with ligand bound exclusively at the alpha haems.
These models were prepared from symmetric, mixed-metal hybrid haemoglobin
molecules. The structures of alpha Fe(II) beta Co(II), its carbonmonoxy
derivative alpha Fe(II)CO beta Co(II), and alpha Fe(II)O2 beta Ni(II) are
compared with native deoxy haemoglobin by difference Fourier syntheses at 2.8,
2.9 and 3.5 A resolution, respectively, and the refined alpha Fe(II)CO beta
Co(II) structure is analysed. In both the native deoxy and liganded T molecules,
the mean plane of the alpha-subunit haem is parallel with the axis of the F
helix, but this plane is tilted with respect to the helix axis in the
oxy-quaternary R state. The side-chains of LeuFG3 and ValFG5 sterically restrict
haem tilting in the T state. We propose that strain energy develops at the
contact between the haem and these residues in the liganded T-state haemoglobin,
and that the strain is, in part, responsible for the low affinity of the T-state
alpha haem.
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Secondary reference #1
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Title
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Stereochemistry of cooperative mechanisms in hemoglobin
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Authors
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M.F.Perutz,
G.Fermi,
B.Luisi,
B.Shaanan,
R.C.Liddington.
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Ref.
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acc chem res, 1987,
20,
309.
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PubMed id
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