The structure of a structural genomics target protein, Tbru020260AAA from Trypanosoma brucei, has been determined to a resolution of 2.2 A using multiple-wavelength anomalous diffraction at the Se K edge. This protein belongs to Pfam sequence family PF08538 and is only distantly related to previously studied members of the alpha/beta-hydrolase fold family. Structural superposition onto representative alpha/beta-hydrolase fold proteins of known function indicates that a possible catalytic nucleophile, Ser116 in the T. brucei protein, lies at the expected location. However, the present structure and by extension the other trypanosomatid members of this sequence family have neither sequence nor structural similarity at the location of other active-site residues typical for proteins with this fold. Together with the presence of an additional domain between strands beta6 and beta7 that is conserved in trypanosomatid genomes, this suggests that the function of these homologs has diverged from other members of the fold family.
George DeTitta合作论文数1Margaret A. Holmes合作论文数1
Eric M. Phizicky合作论文数Department of Biochemistry and Biophysics, University of Rochester Medical Center1Frederick S. Buckner合作论文数1Joseph R. Luft合作论文数Medical Foundation of Buffalo1Angela Lauricella合作论文数1
Wesley C. Van Voorhis (Wesley Van Voorhis)合作论文数Department of Global Health, School of Medicine, University of Washington;Department of Medicine, Division of Allergy and Infectious Diseases, University of Washington;Department of Microbiology, University of Washington;Center for Emerging and Re-emerging Infectious Diseases, University of Washington1Helen Neely合作论文数1
Frank Zucker合作论文数1
Ethan A Merritt (Ethan Merritt)合作论文数Department of Biochemistry, University of Washington;Biomolecular Structure Center, University of Washington1
