Open AccessStructure of Lmaj006129AAA, a hypothetical protein from Leishmania major
Author(s) -
Arakaki Tracy,
Le Trong Isolde,
Phizicky Eric,
Quartley Erin,
DeTitta George,
Luft Joseph,
Lauricella Angela,
Anderson Lori,
Kalyuzhniy Oleksandr,
Worthey Elizabeth,
Myler Peter J.,
Kim David,
Baker David,
Hol Wim G. J.,
Merritt Ethan A.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106005902
Subject(s) - structural genomics , computational biology , molecular replacement , protein structure , sequence (biology) , gene , biology , crystal structure , crystallography , chemistry , genetics , biochemistry
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 ( R free = 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.