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PDBsum entry 1coh
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protein ligands Protein-protein interface(s) links
Oxygen transport PDB id
1coh

 

 

 

 

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Contents
Protein chains
141 a.a. *
146 a.a. *
Ligands
HEM-CMO ×2
COH ×2
Waters ×197
* Residue conservation analysis
PDB id:
1coh
Name: Oxygen transport
Title: Structure of haemoglobin in the deoxy quaternary state with ligand bound at the alpha haems
Structure: Hemoglobin (ferrous carbonmonoxy) (alpha chain). Chain: a, c. Engineered: yes. Hemoglobin (cobaltous deoxy) (beta chain). Chain: b, d. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Organism_taxid: 9606
Biol. unit: Hetero-Tetramer (from PQS)
Resolution:
2.90Å     R-factor:   not given    
Authors: B.Luisi
Key ref: B.Luisi and N.Shibayama (1989). Structure of haemoglobin in the deoxy quaternary state with ligand bound at the alpha haems. J Mol Biol, 206, 723-736. PubMed id: 2738915
Date:
13-Jan-89     Release date:   15-Jan-90    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P69905  (HBA_HUMAN) -  Hemoglobin subunit alpha from Homo sapiens
Seq:
Struc: 		142 a.a.
141 a.a.
Protein chains
Pfam   ArchSchema ?
P68871  (HBB_HUMAN) -  Hemoglobin subunit beta from Homo sapiens
Seq:
Struc: 		147 a.a.
146 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
J Mol Biol 206:723-736 (1989)
PubMed id: 2738915  
 
 
Structure of haemoglobin in the deoxy quaternary state with ligand bound at the alpha haems.
B.Luisi, N.Shibayama.
 
  ABSTRACT  
 
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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18615496 L.L.Kang, Y.X.Huang, W.J.Liu, X.J.Zheng, Z.J.Wu, and M.Luo (2008).
Confocal Raman microscopy on single living young and old erythrocytes.
  Biopolymers, 89, 951-959.  
12023247 L.Mouawad, D.Perahia, C.H.Robert, and C.Guilbert (2002).
New insights into the allosteric mechanism of human hemoglobin from molecular dynamics simulations.
  Biophys J, 82, 3224-3245.  
12146965 S.Nagatomo, M.Nagai, N.Shibayama, and T.Kitagawa (2002).
Differences in changes of the alpha1-beta2 subunit contacts between ligand binding to the alpha and beta subunits of hemoglobin A: UV resonance raman analysis using Ni-Fe hybrid hemoglobin.
  Biochemistry, 41, 10010-10020.  
11976324 U.Samuni, D.Dantsker, I.Khan, A.J.Friedman, E.Peterson, and J.M.Friedman (2002).
Spectroscopically and kinetically distinct conformational populations of sol-gel-encapsulated carbonmonoxy myoglobin. A comparison with hemoglobin.
  J Biol Chem, 277, 25783-25790.  
11604545 S.Bruno, M.Bonaccio, S.Bettati, C.Rivetti, C.Viappiani, S.Abbruzzetti, and A.Mozzarelli (2001).
High and low oxygen affinity conformations of T state hemoglobin.
  Protein Sci, 10, 2401-2407.  
  10794410 S.Bruno, S.Bettati, M.Manfredini, A.Mozzarelli, M.Bolognesi, D.Deriu, C.Rosano, A.Tsuneshige, T.Yonetani, and E.R.Henry (2000).
Oxygen binding by alpha(Fe2+)2beta(Ni2+)2 hemoglobin crystals.
  Protein Sci, 9, 683-692.
PDB code: 1dke
10500299 J.R.Tame (1999).
What is the true structure of liganded haemoglobin?
  Trends Biochem Sci, 24, 372-377.  
9722544 S.Unzai, R.Eich, N.Shibayama, J.S.Olson, and H.Morimoto (1998).
Rate constants for O2 and CO binding to the alpha and beta subunits within the R and T states of human hemoglobin.
  J Biol Chem, 273, 23150-23159.  
  9361418 M.J.Weickert, M.Pagratis, S.R.Curry, and R.Blackmore (1997).
Stabilization of apoglobin by low temperature increases yield of soluble recombinant hemoglobin in Escherichia coli.
  Appl Environ Microbiol, 63, 4313-4320.  
8647851 S.Unzai, H.Hori, G.Miyazaki, N.Shibayama, and H.Morimoto (1996).
Oxygen equilibrium properties of chromium (III)-iron (II) hybrid hemoglobins.
  J Biol Chem, 271, 12451-12456.  
7592833 R.A.Hernan, and S.G.Sligar (1995).
Tetrameric hemoglobin expressed in Escherichia coli. Evidence of heterogeneous subunit assembly.
  J Biol Chem, 270, 26257-26264.  
7873588 Y.Arata (1995).
Effect of the tertiary structure alteration by ligation on the interface contacts between subunits of hemoglobin.
  Biochim Biophys Acta, 1247, 24-34.  
2269272 C.Poyart, O.Schaad, J.Kister, F.Galacteros, S.J.Edelstein, Y.Blouquit, and N.Arous (1990).
Hemoglobin Saint Mandé [beta 102 (G4) Asn----Tyr]. Functional studies and structural modeling reveal an altered T state.
  Eur J Biochem, 194, 343-348.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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