Ontology highlight
ABSTRACT:
SUBMITTER: Escobar-Alvarez S
PROVIDER: S-EPMC2782631 | biostudies-literature | 2009 Apr
REPOSITORIES: biostudies-literature
Escobar-Alvarez Sindy S Goldgur Yehuda Y Yang Guangli G Ouerfelli Ouathek O Li Yueming Y Scheinberg David A DA
Journal of molecular biology 20090221 5
Peptide deformylase proteins (PDFs) participate in the N-terminal methionine excision pathway of newly synthesized peptides. We show that the human PDF (HsPDF) can deformylate its putative substrates derived from mitochondrial DNA-encoded proteins. The first structural model of a mammalian PDF (1.7 A), HsPDF, shows a dimer with conserved topology of the catalytic residues and fold as non-mammalian PDFs. The HsPDF C-terminus topology and the presence of a helical loop (H2 and H3), however, shape ...[more]