| Title |
Structural insight into the specificity of the B3 DNA-binding domains provided by the co-crystal structure of the C-terminal fragment of BfiI restriction enzyme / |
| Authors |
Golovenko, Dmitrij ; Manakova, Elena ; Zakrys, Linas ; Zaremba, Mindaugas ; Sasnauskas, Giedrius ; Gražulis, Saulius ; Šikšnys, Virginijus |
| DOI |
10.1093/nar/gkt1368 |
| Full Text |
|
| Is Part of |
Nucleic acids research.. Oxford : Oxford University Press. 2014, vol. 42, no 6, p. 4113-4122.. ISSN 0305-1048 |
| Abstract [eng] |
The B3 DNA-binding domains (DBDs) of plant transcription factors (TF) and DBDs of EcoRII and BfiI restriction endonucleases (EcoRII-N and BfiI-C) share a common structural fold, classified as the DNA-binding pseudobarrel. The B3 DBDs in the plant TFs recognize a diverse set of target sequences. The only available co-crystal structure of the B3-like DBD is that of EcoRII-N (recognition sequence 50-CCTGG-30). In order to understand the structural and molecular mechanisms of specificity of B3 DBDs, we have solved the crystal structure of BfiI-C (recognition sequence 50-ACTGGG-30) complexed with 12-bp cognate oligoduplex. Structural comparison of BfiI-C–DNA and EcoRII-N–DNA complexes reveals a conserved DNA-binding mode and a conserved pattern of interactions with the phosphodiester backbone. The determinants of the target specificity are located in the loops that emanate from the conserved structural core. The BfiI-C–DNA structure presented here expands a range of templates for modeling of the DNA-bound complexes of the B3 family of plant TFs. |
| Published |
Oxford : Oxford University Press |
| Type |
Journal article |
| Language |
English |
| Publication date |
2014 |
