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PDBsum entry 1lfy

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protein ligands Protein-protein interface(s) links
Oxygen storage/transport PDB id
1lfy
Jmol
Contents
Protein chains
141 a.a. *
146 a.a. *
Ligands
HEM ×2
* Residue conservation analysis
PDB id:
1lfy
Name: Oxygen storage/transport
Title: Oxy hemoglobin (84% relative humidity)
Structure: Hemoglobin alpha chain. Chain: a. Hemoglobin beta chain. Chain: b
Source: Homo sapiens. Human. Organism_taxid: 9606. Organism_taxid: 9606
Biol. unit: Tetramer (from PDB file)
Resolution:
3.30Å     R-factor:   0.208     R-free:   0.261
Authors: B.K.Biswal,M.Vijayan
Key ref:
B.K.Biswal and M.Vijayan (2002). Structures of human oxy- and deoxyhaemoglobin at different levels of humidity: variability in the T state. Acta Crystallogr D Biol Crystallogr, 58, 1155-1161. PubMed id: 12077435 DOI: 10.1107/S0907444902007138
Date:
12-Apr-02     Release date:   12-Oct-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

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

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   9 terms 
  Biological process     small molecule metabolic process   15 terms 
  Biochemical function     protein binding     9 terms  

 

 
DOI no: 10.1107/S0907444902007138 Acta Crystallogr D Biol Crystallogr 58:1155-1161 (2002)
PubMed id: 12077435  
 
 
Structures of human oxy- and deoxyhaemoglobin at different levels of humidity: variability in the T state.
B.K.Biswal, M.Vijayan.
 
  ABSTRACT  
 
High-salt crystals of human oxy- and deoxyhaemoglobin have been studied at different levels of environmental humidity and solvent content. The structure of the oxy form remains relatively unchanged at all levels. The deoxy form, however, undergoes a water-mediated transformation when the relative humidity around the crystals is reduced below 93%. The space group is maintained during the transformation, but the unit-cell volume nearly doubles, with two tetrameric molecules in the asymmetric unit of the low-humidity form compared with one in the native crystals. Interestingly, the haem geometry in the low-humidity form is closer to that in the oxy form than to that in the native deoxy form. The quaternary structure of one of the tetramers moves slightly towards that in the oxy form, while that in the other is more different from the oxy form than that in the high-salt native deoxy form. Thus, it would appear that, as in the case of the liganded form, the deoxy form of haemoglobin can also access an ensemble of related T states.
 
  Selected figure(s)  
 
Figure 3.
Figure 3 The relationship between the unit cells of the native and the low-humidity form of deoxyhaemoglobin. The primed symbols correspond to the low-humidity form.
Figure 4.
Figure 4 Haem environment of the -subunit of native deoxy (red), molecule 1 of deoxy 90% r.h. (blue) and oxy (green) structures.
 
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2002, 58, 1155-1161) copyright 2002.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21543841 V.S.Bhatt, S.Zaldívar-López, D.R.Harris, C.G.Couto, P.G.Wang, and A.F.Palmer (2011).
Structure of Greyhound hemoglobin: origin of high oxygen affinity.
  Acta Crystallogr D Biol Crystallogr, 67, 395-402.
PDB code: 3pel
19659437 T.L.Mollan, X.Yu, M.J.Weiss, and J.S.Olson (2010).
The role of alpha-hemoglobin stabilizing protein in redox chemistry, denaturation, and hemoglobin assembly.
  Antioxid Redox Signal, 12, 219-231.  
17932936 L.Vijayalakshmi, R.Krishna, R.Sankaranarayanan, and M.Vijayan (2008).
An asymmetric dimer of beta-lactoglobulin in a low humidity crystal form--structural changes that accompany partial dehydration and protein action.
  Proteins, 71, 241-249.
PDB codes: 2q2m 2q2p 2q39
  18540052 P.S.Kaushal, R.Sankaranarayanan, and M.Vijayan (2008).
Water-mediated variability in the structure of relaxed-state haemoglobin.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 463-469.
PDB codes: 2zlt 2zlu 2zlv 2zlw 2zlx
15887226 R.Sankaranarayanan, B.K.Biswal, and M.Vijayan (2005).
A new relaxed state in horse methemoglobin characterized by crystallographic studies.
  Proteins, 60, 547-551.
PDB codes: 1y8h 1y8i 1y8k
12524309 A.G.Salvay, J.R.Grigera, and M.F.Colombo (2003).
The role of hydration on the mechanism of allosteric regulation: in situ measurements of the oxygen-linked kinetics of water binding to hemoglobin.
  Biophys J, 84, 564-570.  
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.