2AR1

Structure of Hypothetical protein from Leishmania major

Summary for 2AR1

• Entry DOI: 10.2210/pdb2ar1/pdb
• Descriptor: hypothetical protein, GLYCEROL (3 entities in total)
• Functional Keywords: structural genomics, psi, protein structure initiative, structural genomics of pathogenic protozoa consortium, sgpp, unknown function
• Biological source: Leishmania major
• Total number of polymer chains: 1
• Total formula weight: 20443.40

Authors

Arakaki, T.L.,Merritt, E.A.,Structural Genomics of Pathogenic Protozoa Consortium (SGPP) (deposition date: 2005-08-18, release date: 2005-08-30, Last modification date: 2024-04-03)

Primary citation

Arakaki, T.,Le Trong, I.,Phizicky, E.,Quartley, E.,DeTitta, G.,Luft, J.,Lauricella, A.,Anderson, L.,Kalyuzhniy, O.,Worthey, E.,Myler, P.J.,Kim, D.,Baker, D.,Hol, W.G.,Merritt, E.A.
Structure of Lmaj006129AAA, a hypothetical protein from Leishmania major.
Acta Crystallogr.,Sect.F, 62:175-179, 2006

PubMed 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.

PubMed: 16511295
DOI: 10.1107/S1744309106005902

Experimental method

X-RAY DIFFRACTION (1.602 Å)