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PDBsum entry 1hv4
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protein ligands Protein-protein interface(s) links
Oxygen storage/transport PDB id
1hv4

 

 

 

 

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Contents
Protein chains
141 a.a. *
146 a.a. *
Ligands
HEM ×8
* Residue conservation analysis
PDB id:
1hv4
Name: Oxygen storage/transport
Title: Crystal structure analysis of bar-head goose hemoglobin (deoxy form)
Structure: Hemoglobin alpha-a chain. Chain: a, c, e, g. Hemoglobin beta chain. Chain: b, d, f, h
Source: Anser indicus. Bar-headed goose. Organism_taxid: 8846. Tissue: blood. Cell: erythrocytes. Cellular_location: cytoplasm. Cellular_location: cytoplasm
Biol. unit: Tetramer (from PQS)
Resolution:
2.80Å     R-factor:   0.197     R-free:   0.243
Authors: Y.Liang,Z.Hua,X.Liang,Q.Xu,G.Lu
Key ref:
Y.Liang et al. (2001). The crystal structure of bar-headed goose hemoglobin in deoxy form: the allosteric mechanism of a hemoglobin species with high oxygen affinity. J Mol Biol, 313, 123-137. PubMed id: 11601851 DOI: 10.1006/jmbi.2001.5028
Date:
07-Jan-01     Release date:   17-Jan-01    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P01990  (HBA_ANSIN) -  Hemoglobin subunit alpha-A from Anser indicus
Seq:
Struc: 		142 a.a.
141 a.a.
Protein chains
Pfam   ArchSchema ?
P02118  (HBB_ANSIN) -  Hemoglobin subunit beta from Anser indicus
Seq:
Struc: 		146 a.a.
146 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1006/jmbi.2001.5028 J Mol Biol 313:123-137 (2001)
PubMed id: 11601851  
 
 
The crystal structure of bar-headed goose hemoglobin in deoxy form: the allosteric mechanism of a hemoglobin species with high oxygen affinity.
Y.Liang, Z.Hua, X.Liang, Q.Xu, G.Lu.
 
  ABSTRACT  
 
The crystal structure of a high oxygen affinity species of hemoglobin, bar-headed goose hemoglobin in deoxy form, has been determined to a resolution of 2.8 A. The R and R(free) factor of the model are 0.197 and 0.243, respectively. The structure reported here is a special deoxy state of hemoglobin and indicates the differences in allosteric mechanisms between the goose and human hemoglobins. The quaternary structure of the goose deoxy hemoglobin shows obvious differences from that of human deoxy hemoglobin. The rotation angle of one alphabeta dimer relative to its partner in a tetramer molecule from the goose oxy to deoxy hemoglobin is only 4.6 degrees, and the translation is only 0.3 A, which are much smaller than those in human hemoglobin. In the alpha(1)beta(2) switch region of the goose deoxy hemoglobin, the imidazole ring of His beta(2)97 does not span the side-chain of Thr alpha(1)41 relative to the oxy hemoglobin as in human hemoglobin. And the tertiary structure changes of heme pocket and FG corner are also smaller than that in human hemoglobin. A unique mutation among avian and mammalian Hbs of alpha119 from proline to alanine at the alpha(1)beta(1 )interface in bar-headed goose hemoglobin brings a gap between Ala alpha119 and Leu beta55, the minimum distance between the two residues is 4.66 A. At the entrance to the central cavity around the molecular dyad, some residues of two beta chains form a positively charged groove where the inositol pentaphosphate binds to the hemoglobin. The His beta146 is at the inositol pentaphosphate binding site and the salt-bridge between His beta146 and Asp beta94 does not exist in the deoxy hemoglobin, which brings the weak chloride-independent Bohr effect to bar-headed goose hemoglobin.
 
  Selected figure(s)  
 
Figure 4.
Figure 4. The s[A]-weighted 2F[o] -F[c] map at 1s level around the heme pockets in the a (a) and b (b) subunits of bar-headed goose deoxyHb. 		Figure 7.
Figure 7. Overlapping the goose oxyHb (thin line) and deoxyHb (thick line) on a116-125. Ala a119 contacts with Arg b30 and Ile b33, but has no contacts with Leu b55 in the goose deoxyHb.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (2001, 313, 123-137) copyright 2001.  
  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
20434566 K.G.McCracken, C.P.Barger, and M.D.Sorenson (2010).
Phylogenetic and structural analysis of the HbA (alphaA/betaA) and HbD (alphaD/betaA) hemoglobin genes in two high-altitude waterfowl from the Himalayas and the Andes: Bar-headed goose (Anser indicus) and Andean goose (Chloephaga melanoptera).
  Mol Phylogenet Evol, 56, 649-658.  
19754505 K.G.McCracken, C.P.Barger, M.Bulgarella, K.P.Johnson, S.A.Sonsthagen, J.Trucco, T.H.Valqui, R.E.Wilson, K.Winker, and M.D.Sorenson (2009).
Parallel evolution in the major haemoglobin genes of eight species of Andean waterfowl.
  Mol Ecol, 18, 3992-4005.  
19151158 K.G.McCracken, M.Bulgarella, K.P.Johnson, M.K.Kuhner, J.Trucco, T.H.Valqui, R.E.Wilson, and J.L.Peters (2009).
Gene flow in the face of countervailing selection: adaptation to high-altitude hypoxia in the betaA hemoglobin subunit of yellow-billed pintails in the Andes.
  Mol Biol Evol, 26, 815-827.  
19033139 O.Andersen, O.F.Wetten, M.C.De Rosa, C.Andre, C.Carelli Alinovi, M.Colafranceschi, O.Brix, and A.Colosimo (2009).
Haemoglobin polymorphisms affect the oxygen-binding properties in Atlantic cod populations.
  Proc Biol Sci, 276, 833-841.  
17972287 M.S.Rana, J.E.Knapp, R.A.Holland, and A.F.Riggs (2008).
Component D of chicken hemoglobin and the hemoglobin of the embryonic Tammar wallaby (Macropus eugenii) self-associate upon deoxygenation: Effect on oxygen binding.
  Proteins, 70, 553-561.  
17655497 M.T.Sanna, B.Manconi, G.Podda, A.Olianas, M.Pellegrini, M.Castagnola, I.Messana, and B.Giardina (2007).
Alkaline Bohr effect of bird hemoglobins: the case of the flamingo.
  Biol Chem, 388, 787-795.  
16055861 T.Piersma, J.Pérez-Tris, H.Mouritsen, U.Bauchinger, and F.Bairlein (2005).
Is there a "migratory syndrome" common to all migrant birds?
  Ann N Y Acad Sci, 1046, 282-293.  
15491403 B.Giardina, D.Mosca, and M.C.De Rosa (2004).
The Bohr effect of haemoglobin in vertebrates: an example of molecular adaptation to different physiological requirements.
  Acta Physiol Scand, 182, 229-244.  
11717498 Y.H.Liang, X.Z.Liu, S.H.Liu, and G.Y.Lu (2001).
The structure of greylag goose oxy haemoglobin: the roles of four mutations compared with bar-headed goose haemoglobin.
  Acta Crystallogr D Biol Crystallogr, 57, 1850-1856.
PDB code: 1faw
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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