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PDBsum entry 1lhs

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Oxygen storage PDB id
1lhs

 

 

 

 

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Contents
Protein chain
153 a.a. *
Ligands
HEM
Waters ×63
* Residue conservation analysis
PDB id:
1lhs
Name: Oxygen storage
Title: Loggerhead sea turtle myoglobin (aquo-met)
Structure: Myoglobin. Chain: a. Engineered: yes
Source: Caretta caretta. Loggerhead turtle. Organism_taxid: 8467
Resolution:
2.00Å     R-factor:   0.182    
Authors: M.Nardini,C.Tarricone,A.Lania,A.Desideri,G.De Sanctis,M.Coletta, R.Petruzzelli,P.Ascenzi,A.Coda,M.Bolognesi
Key ref: M.Nardini et al. (1995). Reptile heme protein structure: X-ray crystallographic study of the aquo-met and cyano-met derivatives of the loggerhead sea turtle (Caretta caretta) myoglobin at 2.0 A resolution. J Mol Biol, 247, 459-465. PubMed id: 7714901
Date:
01-Feb-95     Release date:   03-Jun-95    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P56208  (MYG_CARCR) -  Myoglobin from Caretta caretta
Seq:
Struc:
154 a.a.
153 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
J Mol Biol 247:459-465 (1995)
PubMed id: 7714901  
 
 
Reptile heme protein structure: X-ray crystallographic study of the aquo-met and cyano-met derivatives of the loggerhead sea turtle (Caretta caretta) myoglobin at 2.0 A resolution.
M.Nardini, C.Tarricone, M.Rizzi, A.Lania, A.Desideri, G.De Sanctis, M.Coletta, R.Petruzzelli, P.Ascenzi, A.Coda.
 
  ABSTRACT  
 
The X-ray crystal structures of the aquo-met and cyano-met derivatives of the loggerhead sea turtle (Caretta caretta) myoglobin have been determined at 2.0 A resolution (R = 0.182, and 0.178, respectively). The results here reported, representing the first reptile globin solved by X-ray crystallography, have been analyzed in parallel with data for related monomeric hemoproteins, and indicate a strong overall structural similarity between the loggerhead sea turtle and mammalian myoglobins, reflected by the 63% amino acid identity of their primary structures. The root-mean-square deviation between the entire polypeptide backbones of loggerhead sea turtle and sperm whale myoglobins, after structure superposition, is 0.83 A. Upon cyanide binding to the protein distal site, the iron-bound water molecule present in the aquo-met form is displaced by the incoming ligand. Cyanide is oriented towards the inner part of the heme distal site forming a Fe-C-N angle of 133 degrees.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18190529 A.Bolli, C.Ciaccio, M.Coletta, M.Nardini, M.Bolognesi, A.Pesce, M.Guertin, P.Visca, and P.Ascenzi (2008).
Ferrous Campylobacter jejuni truncated hemoglobin P displays an extremely high reactivity for cyanide - a comparative study.
  FEBS J, 275, 633-645.  
  17554165 M.Sugishima, K.Oda, T.Ogura, H.Sakamoto, M.Noguchi, and K.Fukuyama (2007).
Alternative cyanide-binding modes to the haem iron in haem oxygenase.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 471-474.
PDB code: 2e7e
17881827 V.de Serrano, Z.Chen, M.F.Davis, and S.Franzen (2007).
X-ray crystal structural analysis of the binding site in the ferric and oxyferrous forms of the recombinant heme dehaloperoxidase cloned from Amphitrite ornata.
  Acta Crystallogr D Biol Crystallogr, 63, 1094-1101.
PDB codes: 2qfk 2qfn
12192083 D.D.Castelli, E.Lovera, P.Ascenzi, and M.Fasano (2002).
Unfolding of the loggerhead sea turtle (Caretta caretta) myoglobin: A (1)H-NMR and electronic absorbance study.
  Protein Sci, 11, 2273-2278.  
10423453 M.Bolognesi, C.Rosano, R.Losso, A.Borassi, M.Rizzi, J.B.Wittenberg, A.Boffi, and P.Ascenzi (1999).
Cyanide binding to Lucina pectinata hemoglobin I and to sperm whale myoglobin: an x-ray crystallographic study.
  Biophys J, 77, 1093-1099.
PDB codes: 1b0b 1ebc 1ebt
8770225 S.Aime, M.Fasano, S.Paoletti, F.Cutruzzolà, A.Desideri, M.Bolognesi, M.Rizzi, and P.Ascenzi (1996).
Structural determinants of fluoride and formate binding to hemoglobin and myoglobin: crystallographic and 1H-NMR relaxometric study.
  Biophys J, 70, 482-488.  
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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