4KL5

Crystal structure of NpuDnaE intein

Summary for 4KL5

• Entry DOI: 10.2210/pdb4kl5/pdb
• Related: 2KEQ
• Descriptor: DNA polymerase III, alpha subunit, Nucleic acid binding, OB-fold, tRNA/helicase-type chimeric construct, CITRIC ACID, GLYCEROL, ... (4 entities in total)
• Functional Keywords: hint, intein, npudnae inten, unknown function
• Biological source: Nostoc punctiforme; More
• Total number of polymer chains: 2
• Total formula weight: 33231.09

Authors

Aranko, A.S.,Oeemig, J.S.,Kajander, T.,Iwai, H. (deposition date: 2013-05-07, release date: 2013-09-04, Last modification date: 2023-09-20)

Primary citation

Aranko, A.S.,Oeemig, J.S.,Kajander, T.,Iwai, H.
Intermolecular domain swapping induces intein-mediated protein alternative splicing.
Nat.Chem.Biol., 9:616-622, 2013

PubMed Abstract: Protein sequences are diversified on the DNA level by recombination and mutation and can be further increased on the RNA level by alternative RNA splicing, involving introns that have important roles in many biological processes. The protein version of introns (inteins), which catalyze protein splicing, were first reported in the 1990s. The biological roles of protein splicing still remain elusive because inteins neither provide any clear benefits nor have an essential role in their host organisms. We now report protein alternative splicing, in which new protein sequences can be produced by protein recombination by intermolecular domain swapping of inteins, as elucidated by NMR spectroscopy and crystal structures. We demonstrate that intein-mediated protein alternative splicing could be a new strategy to increase protein diversity (that is, functions) without any modification in genetic backgrounds. We also exploited it as a post-translational protein conformation-driven switch of protein functions (for example, as highly specific protein interference).

PubMed: 23974115
DOI: 10.1038/nchembio.1320

Experimental method

X-RAY DIFFRACTION (1.72 Å)