Structure of Lmaj006129AAA, a hypothetical protein from Leishmania major.
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.
Arakaki
Tracy
T
Department of Biochemistry, University of Washington, Seattle, WA 98195-7742, USA.
Le Trong
Isolde
I
Phizicky
Eric
E
Quartley
Erin
E
DeTitta
George
G
Luft
Joseph
J
Lauricella
Angela
A
Anderson
Lori
L
Kalyuzhniy
Oleksandr
O
Worthey
Elizabeth
E
Myler
Peter J
PJ
Kim
David
D
Baker
David
D
Hol
Wim G J
WG
Merritt
Ethan A
EA
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D018320:Leishmania major / Q000737:chemistry*; D015800:Protozoan Proteins / Q000737:chemistry*
D015800:Protozoan Proteins