Structure of Lmaj006129AAA, a hypothetical protein from Leishmania major

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Tracy L ArakakiEthan A Merritt

Abstract

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 A 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.

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Citations

Mar 3, 2007·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Tracy ArakakiEthan A Merritt
May 5, 2010·Journal of Structural Biology·Tracy L ArakakiEthan A Merritt
Feb 5, 2009·Proteins·Claudia BertonatiBurkhard Rost
Jan 25, 2011·Molecular and Biochemical Parasitology·Ethan A MerrittWim G J Hol
Sep 10, 2014·Proceedings of the National Academy of Sciences of the United States of America·Shukun Luo, Liang Tong
Feb 20, 2010·The Journal of Biological Chemistry·Zhaiyi ZhangStefan Stamm
Jan 21, 2010·Journal of Cell Science·Dedreia TullMalcolm J McConville

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