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PDBsum entry 2gzq

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Lipid binding protein PDB id
2gzq

 

 

 

 

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Contents
Protein chain
191 a.a. *
Waters ×282
* Residue conservation analysis
PDB id:
2gzq
Name: Lipid binding protein
Title: Phosphatidylethanolamine-binding protein from plasmodium vivax
Structure: Phosphatidylethanolamine-binding protein. Chain: a. Engineered: yes
Source: Plasmodium vivax. Malaria parasite p. Vivax. Organism_taxid: 5855. Gene: hpf.Pfl0955c. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.30Å     R-factor:   0.161     R-free:   0.180
Authors: T.L.Arakaki,E.A.Merritt,Structural Genomics Of Pathogenic Protozoa Consortium (Sgpp)
Key ref: T.Arakaki et al. (2007). The structure of Plasmodium vivax phosphatidylethanolamine-binding protein suggests a functional motif containing a left-handed helix. Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 178-182. PubMed id: 17329808
Date:
11-May-06     Release date:   23-May-06    
PROCHECK
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 Headers
 References

Protein chain
A5K000  (A5K000_PLAVS) -  Phosphatidylethanolamine-binding protein, putative from Plasmodium vivax (strain Salvador I)
Seq:
Struc:
191 a.a.
191 a.a.*
Key:    Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 

 
Acta Crystallogr Sect F Struct Biol Cryst Commun 63:178-182 (2007)
PubMed id: 17329808  
 
 
The structure of Plasmodium vivax phosphatidylethanolamine-binding protein suggests a functional motif containing a left-handed helix.
T.Arakaki, H.Neely, E.Boni, N.Mueller, F.S.Buckner, W.C.Van Voorhis, A.Lauricella, G.DeTitta, J.Luft, W.G.Hol, E.A.Merritt.
 
  ABSTRACT  
 
The structure of a putative Raf kinase inhibitor protein (RKIP) homolog from the eukaryotic parasite Plasmodium vivax has been studied to a resolution of 1.3 A using multiple-wavelength anomalous diffraction at the Se K edge. This protozoan protein is topologically similar to previously studied members of the phosphatidylethanolamine-binding protein (PEBP) sequence family, but exhibits a distinctive left-handed alpha-helical region at one side of the canonical phospholipid-binding site. Re-examination of previously determined PEBP structures suggests that the P. vivax protein and yeast carboxypeptidase Y inhibitor may represent a structurally distinct subfamily of the diverse PEBP-sequence family.
 

 

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