title: Enhancement of sortase A-mediated protein ligation by inducing a β-hairpin structure around the ligation site.
abstract: A Staphylococcus aureus transpeptidase, sortase A (SrtA), catalyzes selective peptide/protein ligations that have been applied to cell imaging and protein engineering, while the ligations do not proceed to completion due to their reversibility. We successfully enhanced SrtA-mediated protein ligation through the formation of a β-hairpin around the ligation site.
authors.affiliation: Department of Chemistry and Biotechnology, School of Engineering, The University of Tokyo, 7-3-1 Hongo, Tokyo 113-8656, Japan.
authors.forename: Yuichi
authors.initials: Y
authors.lastname: Yamamura
authors.forename: Hidehiko
authors.initials: H
authors.lastname: Hirakawa
authors.forename: Satoshi
authors.initials: S
authors.lastname: Yamaguchi
authors.forename: Teruyuki
authors.initials: T
authors.lastname: Nagamune
mesh_terms: D019881:Aminoacyltransferases / Q000737:chemistry / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D055162:Biocatalysis; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D015202:Protein Engineering; D017433:Protein Structure, Secondary; D011506:Proteins / Q000138:chemical synthesis* / Q000737:chemistry; D013211:Staphylococcus aureus / Q000201:enzymology; D013696:Temperature
chemical_list: D001426:Bacterial Proteins; D011506:Proteins; D019881:Aminoacyltransferases; C120542:sortase A; D003546:Cysteine Endopeptidases