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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. by Golovenko%2c Dmitrij

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1Structural 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.

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This article is from Nucleic Acids Research , volume 42 . Abstract 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 5′-CCTGG-3′). 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 5′-ACTGGG-3′) 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.

“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.” Metadata:

  • 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: ➤  
  • Language: English

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