Structure of Lmaj006129AAA, a hypothetical protein from Leishmania major

Academic Article


  • The gene product of structural genomics target Lmaj006129 from Leishmania major codes for a 164-residue protein of unknown function. When SeMet expression of the full-length gene product failed, several truncation variants were created with the aid of Ginzu, a domain-prediction method. 11 truncations were selected for expression, purification and crystallization based upon secondary-structure elements and disorder. The structure of one of these variants, Lmaj006129AAH, was solved by multiple-wavelength anomalous diffraction (MAD) using ELVES, an automatic protein crystal structure-determination system. This model was then successfully used as a molecular-replacement probe for the parent full-length target, Lmaj006129AAA. The final structure of Lmaj006129AAA was refined to an R value of 0.185 (Rfree = 0.229) at 1.60 Å resolution. Structure and sequence comparisons based on Lmaj006129AAA suggest that proteins belonging to Pfam sequence families PF04543 and PF01878 may share a common ligand-binding motif. © 2006 International Union of Crystallography. All rights reserved.
  • Digital Object Identifier (doi)

    Author List

  • Arakaki T; Le Trong I; Phizicky E; Quartley E; DeTitta G; Luft J; Lauricella A; Anderson L; Kalyuzhniy O; Worthey E
  • Start Page

  • 175
  • End Page

  • 179
  • Volume

  • 62
  • Issue

  • 3