Open AccessThe structure of Plasmodium vivax phosphatidylethanolamine‐binding protein suggests a functional motif containing a left‐handed helix
Author(s) -
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.
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107007580
Subject(s) - motif (music) , crystallography , structural motif , helix (gastropod) , plasmodium vivax , left handed , stereochemistry , biology , chemistry , biophysics , physics , biochemistry , malaria , plasmodium falciparum , zoology , optics , immunology , gastropoda , acoustics
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 Å 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 α‐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.