spacer
spacer

PDBsum entry 1nih
Go to PDB code: 
protein ligands Protein-protein interface(s) links
Oxygen transport PDB id
1nih

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chains
141 a.a. *
146 a.a. *
Ligands
HNI ×2
HEM-CMO ×2
IHP
Waters ×52
* Residue conservation analysis
PDB id:
1nih
Name: Oxygen transport
Title: Structure of deoxy-quaternary haemoglobin with liganded beta subunits
Structure: Hemoglobin (nickelous deoxy) (alpha chain). Chain: a, c. Engineered: yes. Hemoglobin (ferrous carbonmonoxy) (beta chain). Chain: b, d. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Organism_taxid: 9606
Biol. unit: Tetramer (from PQS)
Resolution:
2.60Å     R-factor:   0.214    
Authors: B.Luisi,B.Liddington
Key ref: B.Luisi et al. (1990). Structure of deoxy-quaternary haemoglobin with liganded beta subunits. J Mol Biol, 214, 7. PubMed id: 2370669
Date:
14-Mar-90     Release date:   15-Oct-92    
PROCHECK
Go to PROCHECK summary
 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 214:7 (1990)
PubMed id: 2370669  
 
 
Structure of deoxy-quaternary haemoglobin with liganded beta subunits.
B.Luisi, B.Liddington, G.Fermi, N.Shibayama.
 
  ABSTRACT  
 
We have determined the structure of a T-state haemoglobin in which the haem groups of the beta subunits have carbon monoxide bound, and the alpha subunits have nickel replacing the haem iron and are ligand-free. The structural adjustments on binding ligand in the T state are in the same direction as those associated with the quaternary transition, and a translational shift of the haem is severely restricted. We explain how these observations may account for the low ligand affinity of the beta haem of T-state haemoglobin.
 

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.  
18376851 X.J.Song, V.Simplaceanu, N.T.Ho, and C.Ho (2008).
Effector-induced structural fluctuation regulates the ligand affinity of an allosteric protein: binding of inositol hexaphosphate has distinct dynamic consequences for the T and R states of hemoglobin.
  Biochemistry, 47, 4907-4915.  
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.  
12070336 R.W.Noble, L.D.Kwiatkowski, H.L.Hui, S.Bruno, S.Bettati, and A.Mozzarelli (2002).
Correlation of protein functional properties in the crystal and in solution: the case study of T-state hemoglobin.
  Protein Sci, 11, 1845-1849.  
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.  
12081474 Y.Lu, A.Sousa, R.Franco, A.Mangravita, G.C.Ferreira, I.Moura, and J.A.Shelnutt (2002).
Binding of protoporphyrin IX and metal derivatives to the active site of wild-type mouse ferrochelatase at low porphyrin-to-protein ratios.
  Biochemistry, 41, 8253-8262.  
11566768 A.Riccio, M.Tamburrini, B.Giardina, and G.di Prisco (2001).
Molecular dynamics analysis of a second phosphate site in the hemoglobins of the seabird, south polar skua. Is there a site-site migratory mechanism along the central cavity?
  Biophys J, 81, 1938-1946.  
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.  
10957640 H.C.Wang, Y.H.Liang, J.P.Zhu, and G.Y.Lu (2000).
Crystallization and preliminary crystallographic studies of bar-headed goose fluoromethaemoglobin with inositol hexaphosphate.
  Acta Crystallogr D Biol Crystallogr, 56, 1183-1184.  
  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.  
  9041656 A.Mozzarelli, C.Rivetti, G.L.Rossi, W.A.Eaton, and E.R.Henry (1997).
Allosteric effectors do not alter the oxygen affinity of hemoglobin crystals.
  Protein Sci, 6, 484-489.  
9405399 S.Bettati, and A.Mozzarelli (1997).
T state hemoglobin binds oxygen noncooperatively with allosteric effects of protons, inositol hexaphosphate, and chloride.
  J Biol Chem, 272, 32050-32055.  
9407091 S.Bettati, L.D.Kwiatkowski, J.S.Kavanaugh, A.Mozzarelli, A.Arnone, G.L.Rossi, and R.W.Noble (1997).
Structure and oxygen affinity of crystalline des-his-146beta human hemoglobin in the T state.
  J Biol Chem, 272, 33077-33084.
PDB code: 1axf
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.  
7779259 J.D.Hobbs, and J.A.Shelnutt (1995).
Conserved nonplanar heme distortions in cytochromes c.
  J Protein Chem, 14, 19-25.  
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.  
1896430 F.R.Smith, E.E.Lattman, and C.W.Carter (1991).
The mutation beta 99 Asp-Tyr stabilizes Y--a new, composite quaternary state of human hemoglobin.
  Proteins, 10, 81-91.
PDB code: 1cmy
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.

 

spacer
spacer