Structural highlights
Function
B2J066_NOSP7 B2J821_NOSP7
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Naturally split DnaE intein from Nostoc punctiforme (Npu) has robust protein trans-splicing activity and high tolerance of sequence variations at the splicing junctions. We determined the solution structure of a single chain variant of NpuDnaE intein by NMR spectroscopy. Based on the NMR structure and the backbone dynamics of the single chain NpuDnaE intein, we designed a functional split variant of the NpuDnaE intein having a short C-terminal half (C-intein) composed of six residues. In vivo and in vitro protein ligation of model proteins by the newly designed split intein were demonstrated.
Solution structure of DnaE intein from Nostoc punctiforme: structural basis for the design of a new split intein suitable for site-specific chemical modification.,Oeemig JS, Aranko AS, Djupsjobacka J, Heinamaki K, Iwai H FEBS Lett. 2009 May 6;583(9):1451-6. Epub 2009 Apr 1. PMID:19344715[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Oeemig JS, Aranko AS, Djupsjobacka J, Heinamaki K, Iwai H. Solution structure of DnaE intein from Nostoc punctiforme: structural basis for the design of a new split intein suitable for site-specific chemical modification. FEBS Lett. 2009 May 6;583(9):1451-6. Epub 2009 Apr 1. PMID:19344715 doi:10.1016/j.febslet.2009.03.058
