Structural basis for proteintrans-splicing by a bacterial intein-like domain - protein ligation without nucleophilic side chains

Author:

Aranko A. Sesilja1,Oeemig Jesper S.1,Iwaï Hideo1

Affiliation:

1. Research Program in Structural Biology and Biophysics; Institute of Biotechnology; University of Helsinki; Finland

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference46 articles.

1. Molecular structure of a gene, VMA1, encoding the catalytic subunit of H(+)-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae;Hirata;J Biol Chem,1990

2. Protein splicing converts the yeast TFP1 gene product to the 69-kD subunit of the vacuolar H(+)-adenosine triphosphatase;Kane;Science,1990

3. Protein splicing and related forms of protein autoprocessing;Paulus;Annu Rev Biochem,2000

4. Crystal structure of a hedgehog autoprocessing domain: homology between hedgehog and self-splicing proteins;Hall;Cell,1997

5. Protein splicing of inteins and hedgehog autoproteolysis: structure, function, and evolution;Perler;Cell,1998

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