Structure of Lmaj006129AAA, a hypothetical protein from Leishmania major

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 62; no. 3; pp. 175 - 179
• Main Authors: 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.
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England Munksgaard International Publishers 01.03.2006; International Union of Crystallography
• Subjects: Animals; CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTAL STRUCTURE; CRYSTALLIZATION; Crystallography, X-Ray; DIFFRACTION; FORECASTING; Leishmania major; Leishmania major - chemistry; LENGTH; LIGANDS; Lmaj006129AAA; PROBES; PROTEINS; Protozoan Proteins - chemistry; RESOLUTION; Structural Genomics Communications; WAVELENGTHS
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S1744309106005902

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.