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The structure of Plasmodium vivax phosphatidylethanolamine-binding protein suggests a functional motif containing a left-handed helix.

Authors
  • Arakaki, Tracy
  • Neely, Helen
  • Boni, Erica
  • Mueller, Natasha
  • Buckner, Frederick S
  • Van Voorhis, Wesley C
  • Lauricella, Angela
  • DeTitta, George
  • Luft, Joseph
  • Hol, Wim G J
  • Merritt, Ethan A
Type
Published Article
Journal
Acta Crystallographica Section F Structural Biology and Crystallization Communications
Publisher
International Union of Crystallography
Publication Date
Mar 01, 2007
Volume
63
Issue
Pt 3
Pages
178–182
Identifiers
PMID: 17329808
Source
Medline
License
Unknown

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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